1i10

Ligands:

, ,

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

About this StructureAbout this Structure

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