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2QVH

Crystal structure of O-succinylbenzoate synthase complexed with O-succinyl benzoate (OSB)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0009063biological_processamino acid catabolic process
A0009234biological_processmenaquinone biosynthetic process
A0016829molecular_functionlyase activity
A0016836molecular_functionhydro-lyase activity
A0043748molecular_functionO-succinylbenzoate synthase activity
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0009063biological_processamino acid catabolic process
B0009234biological_processmenaquinone biosynthetic process
B0016829molecular_functionlyase activity
B0016836molecular_functionhydro-lyase activity
B0043748molecular_functionO-succinylbenzoate synthase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 401
ChainResidue
AASP130
AGLU156
AASP179
AOSB5550
AHOH5658

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 400
ChainResidue
BHOH5552
BASP130
BGLU156
BASP179
BOSB5551

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE OSB A 5550
ChainResidue
APHE16
AASN73
ATHR75
ALYS97
AASP130
AASN132
AGLU156
AASP179
ALYS203
ASER227
ASER228
AVAL230
AGLY254
ATHR257
AMG401
AHOH5582
AHOH5583
AHOH5658

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE OSB B 5551
ChainResidue
BPHE16
BASN73
BTHR75
BLYS97
BASP130
BASN132
BGLU156
BASP179
BARG183
BLYS203
BSER227
BSER228
BVAL230
BGLY254
BTHR257
BMG400
BHOH5578
BHOH5587

Functional Information from PROSITE/UniProt
site_idPS00909
Number of Residues32
DetailsMR_MLE_2 Mandelate racemase / muconate lactonizing enzyme family signature 2. VriDvNgawdvdtAvrmirlLdrfeleyVEQP
ChainResidueDetails
AVAL127-PRO158

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00470","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00470","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24060347","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2QVH","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00470","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24060347","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2QVH","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1r6w
ChainResidueDetails
AALA101
ALYS203

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1r6w
ChainResidueDetails
BALA101
BLYS203

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1r6w
ChainResidueDetails
ALYS99
ALYS203

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1r6w
ChainResidueDetails
BLYS99
BLYS203

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PDB entries from 2025-10-29

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