Structure of PDB 1pzg Chain C

Receptor sequence
>1pzgC (length=325) Species: 508771 (Toxoplasma gondii ME49) [Search protein sequence]
ALVQRRKKVAMIGSGMIGGTMGYLCALRELADVVLYDVVKGMPEGKALDL
SHVTSVVDTNVSVRAEYSYEAALTGADCVIVTAGLTKVPGKPDSEWSRND
LLPFNSKIIREIGQNIKKYCPKTFIIVVTNPLDCMVKVMCEASGVPTNMI
CGMACMLDSGRFRRYVADALSVSPRDVQATVIGTHGDCMVPLVRYITVNG
YPIQKFIKDGVVTEKQLEEIAEHTKVSGGEIVRFLGQGSAYYAPAASAVA
MATSFLNDEKRVIPCSVYCNGEYGLKDMFIGLPAVIGGAGIERVIELELN
EEEKKQFQKSVDDVMALNKAVAALQ
3D structure
PDB1pzg Structure of Toxoplasma gondii LDH1: Active-Site Differences from Human Lactate Dehydrogenases and the Structural Basis for Efficient APAD+ Use.
ChainC
Resolution1.6 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) R98 D158 R161 H185
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 SO4 C R109 R171 H195 G236 R98 R161 H185 G228
BS02 A3D C G29 M30 I31 D53 V54 T97 A98 G99 L100 T101 I119 V138 N140 L142 M163 H195 P250 G15 M16 I17 D37 V38 T82 A83 G84 L85 T86 I108 V128 N130 L132 M153 H185 P244 MOAD: Ki=25mM
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:1pzg, PDBe:1pzg, PDBj:1pzg
PDBsum1pzg
PubMed14744130
UniProtP90613

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