Structure of PDB 1pzh Chain D

Receptor sequence
>1pzhD (length=326) Species: 508771 (Toxoplasma gondii ME49) [Search protein sequence]
PALVQRRKKVAMIGSGMIGGTMGYLCALRELADVVLYDVVKGMPEGKALD
LSHVTSVVDTNVSVRAEYSYEAALTGADCVIVTAGLTKVPGKPDSEWSRN
DLLPFNSKIIREIGQNIKKYCPKTFIIVVTNPLDCMVKVMCEASGVPTNM
ICGMACMLDSGRFRRYVADALSVSPRDVQATVIGTHGDCMVPLVRYITVN
GYPIQKFIKDGVVTEKQLEEIAEHTKVSGGEIVRFLGQGSAYYAPAASAV
AMATSFLNDEKRVIPCSVYCNGEYGLKDMFIGLPAVIGGAGIERVIELEL
NEEEKKQFQKSVDDVMALNKAVAALQ
3D structure
PDB1pzh Structure of Toxoplasma gondii LDH1: Active-Site Differences from Human Lactate Dehydrogenases and the Structural Basis for Efficient APAD+ Use.
ChainD
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) R99 D159 R162 H186
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 D W107 R109 R171 H195 G236 W97 R99 R162 H186 G229
BS02 NAD D G29 M30 I31 D53 V54 T97 A98 G99 L100 T101 I119 V138 N140 M163 H195 G16 M17 I18 D38 V39 T83 A84 G85 L86 T87 I109 V129 N131 M154 H186
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:1pzh, PDBe:1pzh, PDBj:1pzh
PDBsum1pzh
PubMed14744130
UniProtP90613

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