Structure of PDB 2a92 Chain A

Receptor sequence
>2a92A (length=316) Species: 5855 (Plasmodium vivax) [Search protein sequence]
TPKPKIVLVGSGMIGGVMATLIVQKNLGDVVMFDVVKNMPQGKALDTSHS
NVMAYSNCKVTGSNSYDDLKGADVVIVTAGFTKAPGKSDKEWNRDDLLPL
NNKIMIEIGGHIKNLCPNAFIIVVTNPVDVMVQLLFEHSGVPKNKIIGLG
GVLDTSRLKYYISQKLNVCPRDVNALIVGAHGNKMVLLKRYITVGGIPLQ
EFINNKKITDEEVEGIFDRTVNTALEIVNLLASPYVAPAAAIIEMAESYL
KDIKKVLVCSTLLEGQYGHSNIFGGTPLVIGGTGVEQVIELQLNAEEKTK
FDEAVAETKRMKALIH
3D structure
PDB2a92 Structure of Lactate Dehydrogenase from Plasmodium vivax: Complexes with NADH and APADH.
ChainA
Resolution2.04 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R109 D168 R171 H195
Catalytic site (residue number reindexed from 1) R94 D154 R157 H181
Enzyme Commision number 1.1.1.27: L-lactate dehydrogenase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 NAI A G29 M30 I31 F52 D53 V54 Y85 T97 A98 I119 V138 N140 V142 L163 L167 H195 G12 M13 I14 F33 D34 V35 Y66 T78 A79 I104 V124 N126 V128 L149 L153 H181
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003824 catalytic activity
GO:0004459 L-lactate dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Biological Process
GO:0006089 lactate metabolic process
GO:0006090 pyruvate metabolic process
GO:0019752 carboxylic acid metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2a92, PDBe:2a92, PDBj:2a92
PDBsum2a92
PubMed16331982
UniProtQ4PRK9

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