Structure of PDB 1oc4 Chain A

Receptor sequence
>1oc4A (length=315) Species: 5821 (Plasmodium berghei) [Search protein sequence]
APKAKIVLVGSGMIGGVMATLIVQKNLGDVVMFDIVKNMPHGKALDTSHT
NVMAYSNCKVSGSNTYDDLKDADVVIVTAGFTKAPGKSDKEWNRDDLLPL
NNKIMIEIGGHIKNNCPNAFIIVVTNPVDVMVQLLHQHSGVPKNKIVGLG
GVLDTSRLKYYISQKLNVCPRDVNAHIVGAHGNKMVLLKRYITVGGIPLQ
EFINNKKITDQELDAIFDRTINTALEIVNLHASPYVAPAAAIIEMAESYI
RDLRKVLICSTLLEGQYGHKDIFAGTPLVIGGNGVEQVIELQLNADEKKK
FDEAVAETSRMKALI
3D structure
PDB1oc4 Crystal Structure of Plasmodium Berghei Lactate Dehydrogenase Indicates the Unique Structural Differences of These Enzymes are Shared Across the Plasmodium Genus
ChainA
Resolution2.3 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 NAD A G27 G29 M30 I31 F52 D53 I54 Y85 T97 A98 G99 F100 T101 V138 N140 L163 L167 H195 G10 G12 M13 I14 F33 D34 I35 Y66 T78 A79 G80 F81 T82 V124 N126 L149 L153 H181
Gene Ontology
Molecular Function
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
GO:0051287 NAD binding
Biological Process
GO:0006089 lactate metabolic process
GO:0006090 pyruvate metabolic process
GO:0006096 glycolytic process
GO:0019752 carboxylic acid metabolic process
GO:0042866 pyruvate biosynthetic process

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Molecular Function

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Biological Process
External links
PDB RCSB:1oc4, PDBe:1oc4, PDBj:1oc4
PDBsum1oc4
PubMed12967707
UniProtQ7SI97|LDH_PLABA L-lactate dehydrogenase (Gene Name=LDH)

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