Structure of PDB 3czm Chain A

Receptor sequence
>3czmA (length=322) Species: 5811 (Toxoplasma gondii) [Search protein sequence]
TVSRRKKIAMIGSGMIGGTMGYLCVLRELADVVLFDVVTGMPEGKALDDS
QATSIADTNVSVTSANQYEKIAGSDVVIITAGLTKVPGKSDKEWSRNDLL
PFNAKIIREVAQGVKKYCPLAFVIVVTNPLDCMVKCFHEASGLPKNMVCG
MANVLDSARFRRFIADQLEISPRDIQATVIGTHGDHMLPLARYVTVNGFP
LREFIKKGKMTEAKLAEIVERTKKAGGEIVRLLGQGSAYYAPALSAITMA
QAFLKDEKRVLPCSVYCQGEYGLHDMFIGLPAVIGGGGIEQVIELELTHE
EQECFRKSVDDVVELNKSLAAL
3D structure
PDB3czm T. Gondii bradyzoite-specific LDH (LDH2) in complex with NAD and OXQ
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) R96 D156 R159 H183
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 G29 M30 I31 D53 V54 T97 A98 G99 L100 T101 I119 V138 N140 M163 H195 G14 M15 I16 D36 V37 T80 A81 G82 L83 T84 I106 V126 N128 M151 H183
BS02 OXQ A W107 R109 N140 R171 H195 G236 S245 W94 R96 N128 R159 H183 G226 S237
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
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:3czm, PDBe:3czm, PDBj:3czm
PDBsum3czm
PubMed
UniProtQ27797|LDH_TOXGO L-lactate dehydrogenase

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