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2V7B

Crystal structures of a benzoate CoA ligase from Burkholderia xenovorans LB400

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0016020cellular_componentmembrane
A0016405molecular_functionCoA-ligase activity
A0016874molecular_functionligase activity
A0016878molecular_functionacid-thiol ligase activity
A0018858molecular_functionbenzoate-CoA ligase activity
A0044550biological_processsecondary metabolite biosynthetic process
B0005524molecular_functionATP binding
B0016020cellular_componentmembrane
B0016405molecular_functionCoA-ligase activity
B0016874molecular_functionligase activity
B0016878molecular_functionacid-thiol ligase activity
B0018858molecular_functionbenzoate-CoA ligase activity
B0044550biological_processsecondary metabolite biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE BEZ A 1529
ChainResidue
APHE236
AHOH2547
ATYR238
AALA308
AGLY309
AGLY333
ASER334
AHIS339
ALYS520
AHOH2546

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE BEZ B 1529
ChainResidue
BPHE236
BTYR238
BALA308
BGLY309
BGLY333
BSER334
BHIS339
BLYS520
BHOH2311
BHOH2515

Functional Information from PROSITE/UniProt
site_idPS01039
Number of Residues14
DetailsSBP_BACTERIAL_3 Bacterial extracellular solute-binding proteins, family 3 signature. GYEIELRDeAGHAV
ChainResidueDetails
AGLY360-VAL373

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PDB entries from 2025-07-30

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