Structure of PDB 2hjr Chain J

Receptor sequence
>2hjrJ (length=314) Species: 5807 (Cryptosporidium parvum) [Search protein sequence]
MRKKISIIGAGQIGSTIALLLGQKDLGDVYMFDIIEGVPQGKALDLNHCM
ALIGSPAKIFGENNYEYLQNSDVVIITAGVPRKPNMTRSDLLTVNAKIVG
SVAENVGKYCPNAFVICITNPLDAMVYYFKEKSGIPANKVCGMSGVLDSA
RFRCNLSRALGVKPSDVSAIVVGGHGDEMIPLTSSVTIGGILLSDFVEQG
KITHSQINEIIKKTAFGGGEIVELLKTGSAFYAPAASAVAMAQAYLKDSK
SVLVCSTYLTGQYNVNNLFVGVPVVIGKNGIEDVVIVNLSDDEKSLFSKS
VESIQNLVQDLKSL
3D structure
PDB2hjr Genome-scale protein expression and structural biology of Plasmodium falciparum and related Apicomplexan organisms.
ChainJ
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R100 D160 R163 H187
Catalytic site (residue number reindexed from 1) R88 D148 R151 H175
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 APR J G23 Q24 I25 D45 I46 I47 Y77 A90 G91 V92 T131 N132 G11 Q12 I13 D33 I34 I35 Y65 A78 G79 V80 T119 N120
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:2hjr, PDBe:2hjr, PDBj:2hjr
PDBsum2hjr
PubMed17125854
UniProtQ5CYZ3

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