Structure of PDB 1sow Chain A

Receptor sequence
>1sowA (length=322) Species: 5811 (Toxoplasma gondii) [Search protein sequence]
TVSRRKKIAMIGSGMIGGTMGYLCVLRELADVVLFDVVTGMPEGKALDDS
QATSIADTNVSVTSANQYEKIAGSDVVIITAGLTKVPGKSDKEWSRNDLL
PFNAKIIREVAQGVKKYCPLAFVIVVTNPLDCMVKCFHEASGLPKNMVCG
MANVLDSARFRRFIADQLEISPRDIQATVIGTHGDHMLPLARYVTVNGFP
LREFIKKGKMTEAKLAEIVERTKKAGGEIVRLLGQGSAYYAPALSAITMA
QAFLKDEKRVLPCSVYCQGEYGLHDMFIGLPAVIGGGGIEQVIELELTHE
EQECFRKSVDDVVELNKSLAAL
3D structure
PDB1sow Structure of apo and ternary forms of Toxoplasma gondii LDH2
ChainA
Resolution1.9 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 OXL A W107 R109 R171 H195 G236 W94 R96 R159 H183 G226
BS02 NAD A G29 M30 I31 D53 V54 T97 A98 G99 L100 T101 I119 E122 V138 T139 N140 M163 L167 H195 P250 G14 M15 I16 D36 V37 T80 A81 G82 L83 T84 I106 E109 V126 T127 N128 M151 L155 H183 P242
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:1sow, PDBe:1sow, PDBj:1sow
PDBsum1sow
PubMed
UniProtQ27797|LDH_TOXGO L-lactate dehydrogenase

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