Structure of PDB 2hjr Chain L

Receptor sequence
>2hjrL (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.
ChainL
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 L G23 Q24 I25 D45 I46 I47 Y77 A90 P93 I110 I130 T131 N132 G11 Q12 I13 D33 I34 I35 Y65 A78 P81 I98 I118 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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2hjr, PDBe:2hjr, PDBj:2hjr
PDBsum2hjr
PubMed17125854
UniProtQ5CYZ3

[Back to BioLiP]