1i10 | pdb_00001i10

1i10, resolution 2.30Å (default scene)

Ligands:

ACT, NAI, OXM

Gene:

LDHA (Homo sapiens)

Activity:

L-lactate dehydrogenase, with EC number 1.1.1.27

Related:

1i0z, 9ldt, 5ldh, 1ldg

Structural annotation:
Resources:	CATH : 1I10A02, 1I10A01, 1I10B01, 1I10B02, 1I10C02, 1I10C01, 1I10D01, 1I10D02, 1I10E02, 1I10E01, 1I10F01, 1I10F02, 1I10G02, 1I10G01, 1I10H01, 1I10H02 InterPro : Ipr001557, Ipr001236, Ipr011304 Pfam : PF00056, PF02866 SCOP : d1i10a1, d1i10a2, d1i10b2, d1i10b1, d1i10c2, d1i10c1, d1i10d1, d1i10d2, d1i10e1, d1i10e2, d1i10f1, d1i10f2, d1i10g2, d1i10g1, d1i10h2, d1i10h1 UniProt : P00338

Functional annotation:
Cellular component:	cytosol cytoplasm
Biological process:	anaerobic glycolysis cellular carbohydrate metabolic process glycolysis tricarboxylic acid cycle intermediate metabolic process
Molecular function:	L-lactate dehydrogenase activity oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor oxidoreductase activity protein binding

Evolutionary conservation:

Toggle Conservation Colors:	Rows = identical sequences:
Further Information:	Caveats, Explanation, Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, RCSB, PDBsum

Coordinates:

save as pdb, mmCIF, xml

HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE

Template:ABSTRACT PUBMED 11276087

Disease

[LDHA_HUMAN] Defects in LDHA are the cause of glycogen storage disease type 11 (GSD11) [MIM:612933]. A metabolic disorder that results in exertional myoglobinuria, pain, cramps and easy fatigue.^[1]

About this Structure

1i10 is a 8 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Read JA, Winter VJ, Eszes CM, Sessions RB, Brady RL. Structural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenase. Proteins. 2001 May 1;43(2):175-85. PMID:11276087

↑ Maekawa M, Sudo K, Kanno T, Li SS. Molecular characterization of genetic mutation in human lactate dehydrogenase-A (M) deficiency. Biochem Biophys Res Commun. 1990 Apr 30;168(2):677-82. PMID:2334430

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OCA

[1] Read JA, Winter VJ, Eszes CM, Sessions RB, Brady RL. Structural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenase. Proteins. 2001 May 1;43(2):175-85. PMID:11276087

[1] Maekawa M, Sudo K, Kanno T, Li SS. Molecular characterization of genetic mutation in human lactate dehydrogenase-A (M) deficiency. Biochem Biophys Res Commun. 1990 Apr 30;168(2):677-82. PMID:2334430

[1]

1i10 | pdb_00001i10

Contents

HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE

Disease

About this Structure

See Also

Reference

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