Structure of PDB 6o0j Chain A

Receptor sequence
>6o0jA (length=527) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
MNPSTTQARVVVDELIRGGVRDVVLCPGSRNAPLAFALQDADRSGRIRLH
VRIDERTAGYLAIGLAIGAGAPVCVAMTSGTAVANLGPAVVEANYARVPL
IVLSANRPYELLGTGANQTMEQLGYFGTQVRASISLGLAEDAPERTSALN
ATWRSATCRVLAAATGARTANAGPVHFDIPLREPLVPDPPLVTPPGRPAG
KPWTYTPPVTFDQPLDIDLSVDTVVISGHGAGVHPNLAALPTVAEPTAPR
SGDNPLHPLALPLLRPQQVIMLGRPTLHRPVSVLLADAEVPVFALTTGPR
WPDVSGNSQATGTRAVTTGAPRPAWLDRCAAMNRHAIAAVREQLAAHPLT
TGLHVAAAVSHALRPGDQLVLGASNPVRDVALAGLDTRGIRVRSNRGVAG
IDGTVSTAIGAALAYEGAHERTDSPPRTIALIGDLTFVHDSSGLLIGPTE
PIPRSLTIVVSNDNGGVSSRIFHDVDVGALCRAYHVESRQIEVDELGPTL
DQGMRVLEVKADRSSLRQLHAAIKAAL
3D structure
PDB6o0j Allosteric regulation of menaquinone (vitamin K2) biosynthesis in the human pathogenMycobacterium tuberculosis.
ChainA
Resolution2.35 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.2.1.9: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase.
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 DNA A Y95 R97 R277 R303 W304 P305 Y95 R97 R274 R300 W301 P302
BS02 TPP A P27 E55 T78 P27 E55 T78
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0016740 transferase activity
GO:0030145 manganese ion binding
GO:0030976 thiamine pyrophosphate binding
GO:0046872 metal ion binding
GO:0070204 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase activity
Biological Process
GO:0009234 menaquinone biosynthetic process
Cellular Component
GO:0005886 plasma membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6o0j, PDBe:6o0j, PDBj:6o0j
PDBsum6o0j
PubMed32029475
UniProtP9WK11|MEND_MYCTU 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase (Gene Name=menD)

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