Structure of PDB 3h3j Chain B

Receptor sequence
>3h3jB (length=314) Species: 93062 (Staphylococcus aureus subsp. aureus COL) [Search protein sequence]
FKGNKVVLIGNGAVGSSYAFSLVNQSIVDELVIIDLDTEKVRGDVMDLKH
ATPYSPTTVRVKAGEYSDCHDADLVVICAGARQKPGETRLDLVSKNLKIF
KSIVGEVMASKFDGIFLVATNPVDILAYATWKFSGLPKERVIGSGTILDS
ARFRLLLSEAFDVAPRSVDAQIIGEHGDTELPVWSHANIAGQPLKTLLEQ
RPEGKAQIEQIFVQTRDAAYDIIQAKGATYYGVAMGLARITEAIFRNEDA
VLTVSALLEGEYEEEDVYIGVPAVINRNGIRNVVEIPLNDEEQSKFAHSA
KTLKDIMAEAEELK
3D structure
PDB3h3j Crystal structure of lactate dehydrogenase mutant (A85R) from staphylococcus aureus complexed with NAD and pyruvate
ChainB
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R92 D152 R155 H179
Catalytic site (residue number reindexed from 1) R89 D149 R152 H176
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 NAD B G15 A16 V17 D38 L39 C81 A82 G83 A84 R85 A122 N124 H179 T232 V236 G12 A13 V14 D35 L36 C78 A79 G80 A81 R82 A119 N121 H176 T229 V233
BS02 PYR B R92 N124 L151 R155 H179 A222 T232 R89 N121 L148 R152 H176 A219 T229
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:0006096 glycolytic process
GO:0019752 carboxylic acid metabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:3h3j, PDBe:3h3j, PDBj:3h3j
PDBsum3h3j
PubMed
UniProtQ5HJD7|LDH1_STAAC L-lactate dehydrogenase 1 (Gene Name=ldh1)

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