1i10: Difference between revisions

Revision as of 12:39, 26 July 2012

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

1i10 is a 8 chain structure of Flavodoxin and Lactate Dehydrogenase with sequence from Homo sapiens. Full crystallographic information is available from OCA.

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

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