Chitinase
From Proteopedia
Revision as of 08:45, 10 April 2018 by Michal Harel (talk | contribs)
ContentsFunctionChitinases cleave the beta-1-4-glycosidic bond between the N-acetyl-D-glucosamine units of which chitin is comprised. Chitinases are present in plants, bacteria and fungi. The first chitinase structures were solved in 1994, from a bacterium (1ctn) and a plant (2hvm). A mechanism for chitin cleavage was proposed based on several structures and was later confirmed. [1] DiseaseChi is related to allergies and asthma. Structural highlightsThe chitin tetrasaccharide binding site of Chitinase A.[2]
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3D Structures of Chitinase
Updated on 10-April-2018
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- Chitinase I
- 1ctn, 2hvm – VhChi residues 22-597 – Vibrio harveyi
- 3b9e - VhChi residues 22-597 (mutant)
- 1k85 – BcChi fibronectin domain – Bacillus circulans – NMR
- 1itx - BcChi catalytic domain
- 1ed7 – BcChi chitin-binding domain - NMR
- 1ll6, 1ll7 - CiChi residues 36-427 (mutant) – Coccicioides immitis
- 1d2k - CiChi residues 36-427
- 3n11 – BcChi – Bacillus cereus
- 3iwr, 2dkv – Chi residues 33-340 – Japanese rice
- 3g6l - BoChi residues 21-426 – Bionectria ochroleuca
- 3oa5, 4dws – Chi – Yersinia entomophaga
- 4mpi – HbChi chitin-binding domain – Hevea brasiliensis
- 4mst – HbChi catalytic domain
- 4wjx, 4wka – hChi catalytic domain - human
- 4tx7 – Chi – yard-long bean
- 1ctn, 2hvm – VhChi residues 22-597 – Vibrio harveyi
- Chitinase I binary complex
- 3arp, 3arq, 3arr, 3ars, 3art, 3aru, 3arv, 3arw, 3arx, 3ary, 3arz – VhChi residues 22-597 + inhibitor
- 3as0, 3as1, 3as2, 3as3 – VhChi residues 22-597 (mutant) + inhibitor
- 3b9a, 3b9d - VhChi residues 22-597 + polysaccharide
- 2xvn, 2xuc – AfChi residues 29-307 + inhibitor – Aspergillus fumigatus
- 3n13, 3n15, 3n17, 3n18 – BcChi (mutant) + NAG
- 3n12 – BcChi + Zn
- 3n1a - BcChi (mutant) + inhibitor
- 3g6m - BoChi residues 21-426 + caffeine
- 1waw, 1wb0, 4wk9, 4wkf, 4wkh – hChi catalytic domain + polypeptide – human
- 1hkk, 1hkm, 3rm4, 3rm8, 3rm9, 3rme – hChi catalytic domain + inhibitor
- 1ll4 - CiChi residues 36-427 + inhibitor
- 3wl1, 3wqv, 3wqw – cbChi + GlcNAC
- 3wl0 – cbChi (mutant) + GlcNAC
- 3arp, 3arq, 3arr, 3ars, 3art, 3aru, 3arv, 3arw, 3arx, 3ary, 3arz – VhChi residues 22-597 + inhibitor
- Chitinase II
- Chitinase II binary complex
- 1ogg, 1ur9 - SmChi (mutant) + inhibitor
- 1e6n - SmChi (mutant) + polysaccharide
- 1ur8, 1gpf, 1e6r, 3wd1, 3wd2, 3wd3, 3wd4 - SmChi + inhibitor
- 1e6z – SmChi + intermediate
- 2a3a, 2a3b, 2a3c, 2a3e – AfChi + inhibitor
- 1w1p, 1w1t, 1w1v, 1w1y, 1o6i, 1h0g, 1h0i – SmChi + polypeptide
- 5y2b – OfChi catalytic domain 1 + acetylchitooctaose
- 5y2c – OfChi catalytic domain 2 (mutant) + acetylchitooctaose
- 1ogg, 1ur9 - SmChi (mutant) + inhibitor
- Chitinase III
- 2dbt, 1wvu – SgChi residues 30-294 – Streptomyces griseus
- 1wvv - SgChi residues 30-294 (mutant)
- 2d49 – SgChi chitin-binding domain - NMR
- 2xvp – AfChi
- 2xtk, 4tx6 – AfChi + inhibitor
- 4toq – Chi - pomegrenate
- 5wup – OfChi residues 1-482
- 5wv8 – OfChi residues 1-482 (mutant)
- 5wv9 – OfChi residues 1-482 + GlcNAc
- 5wvb – OfChi residues 1-482 (mutant) + GlcNAc
- 5wus – OfChi residues 528-987
- 5wvf – OfChi residues 528-987 (mutant)
- 5wvh – OfChi residues 528-987 + GlcNAc
- 5wvg – OfChi residues 528-987 (mutant) + GlcNAc
- 2dbt, 1wvu – SgChi residues 30-294 – Streptomyces griseus
- Chitinase IV
- Chitinase V
- 3alf – tChi residues 26-377 – tobacco
- 3alf – tChi residues 26-377 – tobacco
- Chitinase V binary complex
- Chitinase VIII
- 2cjl - Chi residues 41-244 – Streptomyces coelicolor
- 2cjl - Chi residues 41-244 – Streptomyces coelicolor
- Chitinase XVIII
- 3sim – Chi – Crocus vernus
- Chitinase A
- 3wh1, 3wij – BcChiA + GlcNAC – Bryum coronatum
- 4ij4 – BcChiA (mutant) + GlcNAC
- 4mnj, 4r5e – spChiA – sago palm
- 4mnk – spChiA + GlcNAC
- 4mnl, 4mnm – spChiA (mutant) + GlcNAC
- 5dez – ApChiA + NAG – Autographa polyhedrosis
- 5df0 – ApChiA + NAG + chitotriothiazoline
- 5bum – ChiA LYSM domain – field horsetail
- 1edq, 1ctn - SmChiA – Serratia marcescens
- 1x6l, 1rd6 – SmChiA (mutant)
- 1x6n - SmChi (mutant) + inhibitor
- 1ffq, 2wk2, 2wly, 2wlz, [[[2wm0]] - SmChi + inhibitor
- 1nh6, 1k9t, 1ffr, 1eib, 1ehn - SmChi (mutant) + polysaccharide
- 4pxv – PrChiA LYSM domain – Pteris ryukuensis
- 4rl3 – PrChiA catalytic domain
- 3wh1, 3wij – BcChiA + GlcNAC – Bryum coronatum
- Chitinase B
- Chitinase C
- Chitinase H
- Other chitinases
- 1wno, 1w9p - AfChi
- 2dsk - PfChi catalytic domain – Pyrococcus furiosus
- 3afb - PfChi catalytic domain (mutant)
- 1cns – Chi – Hordeum vulgare
- 2czn, 2rts - PfChi chitin-binding domain – NMR
- 2cwr - PfChi chitin-binding domain
- 3ian – Chi (mutant) – Lactococcus lactis
- 3fxy - hChi catalytic domain
- 1lq0 - hChi residues 22-286
- 1guv - hChi residues 22-387
- 3fnd, 3co4 – Chi – Bacteroides thetaiotamicron
- 3cql – Chi – Carica papaya
- 2z37 - BjChi catalytic domain – Brassica juncea
- 2z39 – BjChi catalytic domain (mutant)
- 2uy2 – yChi residues 22-315 – yeast
- 4hmc – MmChi 60 – Moritella marina
- 4mb3 – MmChi 60 (mutant)
- 3w3e – Chi – cowpea
- 3w6b – RaChi catalytic domain – Ralstonia
- 3w6e – RaChi catalytic domain (mutant)
- 4w5z – Chi 60 catalytic domain – Vibrio marinus
- 5kz6 – Chi – Bacillus anthracis
- 5gzt, 5gzv, 5gzu – ChiW – Paeniacillus
- 5dhd – TkChi CHBD2 domain – Thermococcus kodakarensis
- 5dhe – TkChi CHBD3 domain
- 5aa7 – Chi polusaccharide monooxygenase domain – Jonesia dentrificans
- 4w5u – Chi 40 – Streptomyces thermoviolaceus
- 4txg – Chi – Chromobacterium violaceum
- 5vg0 – JdChi – Jonesia denitrificans
- 5vg1 – JdChi – Neutron
- 5k2l – Chi LYSM domain – Volvox carteri
- 1wno, 1w9p - AfChi
- Other chitinases binary complex
- 3a4w, 3a4x – PfChi catalytic domain (mutant) + NAG
- 1lg1 - hChi residues 22-387 + chitobiose
- 1lg2 - hChi residues 22-387 + ethylene glycol
- 3fy1, 2ybt, 2ybu - hChi catalytic domain + inhibitor
- 1hki, 1hkj - hChi + inhibitor
- 2z38 - BjChi catalytic domain + Cl
- 2uy3, 2uy4, 2uy5 - yChi residues 22-315 + inhibitor
- 1w9v, 1w9u - AfChi + polypeptide
- 4hmd – MmChi 60 + intermediate
- 4hme – MmChi 60 + NAG
- 4mb4, 4mb5 – MmChi 60 (mutant) + NAG
- 3w6c – RaChi catalytic domain + disaccharide
- 3w6d, 3w6f – RaChi catalytic domain (mutant) + polysaccharide
- 3a4w, 3a4x – PfChi catalytic domain (mutant) + NAG
References
Proteopedia Page Contributors and Editors (what is this?)
Alexander Berchansky, Anastassis Perrakis, Marcin Jozef Suskiewicz, Michal Harel
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