1i10 | pdb_00001i10

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

Template:ABSTRACT PUBMED 11276087

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

Disease

Known disease associated with this structure: Exertional myoglobinuria due to deficiency of LDH-A OMIM:[150000]

About this Structure

1I10 is a 8 chains structure of sequences 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

Page seeded by OCA on Tue Feb 17 09:19:04 2009

Proteopedia Page Contributors and Editors (what is this?)

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

1i10 | pdb_00001i10

Contents

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

Disease

About this Structure

Reference

Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools