Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2VGR

Structure of the WT-Phycoerythrobilin Synthase PebS from the Cyanophage P-SSM2 in Complex with the bound Substrate Biliverdin IXa

Functional Information from GO Data
ChainGOidnamespacecontents
A0010024biological_processphytochromobilin biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016636molecular_functionoxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor
A0050619molecular_functionphytochromobilin:ferredoxin oxidoreductase activity
A0050897molecular_functioncobalt ion binding
B0010024biological_processphytochromobilin biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0016636molecular_functionoxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor
B0050619molecular_functionphytochromobilin:ferredoxin oxidoreductase activity
B0050897molecular_functioncobalt ion binding
C0010024biological_processphytochromobilin biosynthetic process
C0016491molecular_functionoxidoreductase activity
C0016636molecular_functionoxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor
C0050619molecular_functionphytochromobilin:ferredoxin oxidoreductase activity
C0050897molecular_functioncobalt ion binding
D0010024biological_processphytochromobilin biosynthetic process
D0016491molecular_functionoxidoreductase activity
D0016636molecular_functionoxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor
D0050619molecular_functionphytochromobilin:ferredoxin oxidoreductase activity
D0050897molecular_functioncobalt ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE BLA A1234
ChainResidue
AILE79
ATYR158
AMET202
AASP206
APRO207
AVAL208
ATYR211
AASN88
AASP105
AMET107
APHE109
AILE115
ATYR141
APHE143
APHE144

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE BLA B1234
ChainResidue
BILE79
BILE86
BASN88
BGLY103
BMET104
BASP105
BMET107
BPHE109
BVAL117
BGLN121
BARG142
BPHE143
BTYR158
BMET202
BASP206
BVAL208
BTYR211

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE BLA C1234
ChainResidue
CILE79
CASN88
CASP105
CMET107
CPHE109
CILE115
CTYR141
CPHE143
CPHE144
CTYR158
CMET202
CLEU205
CASP206
CPRO207
CVAL208
CTYR211
CPHE230

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE BLA D1234
ChainResidue
DILE79
DASN88
DILE90
DGLY103
DMET104
DASP105
DMET107
DPHE109
DVAL117
DGLN121
DARG142
DPHE143
DTYR158
DMET202
DPRO207
DTYR211
DHOH2077

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 306
ChainResidueDetails
AASP105hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, steric role
AASP206hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_idMCSA2
Number of Residues2
DetailsM-CSA 306
ChainResidueDetails
BASP105hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, steric role
BASP206hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_idMCSA3
Number of Residues2
DetailsM-CSA 306
ChainResidueDetails
CASP105hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, steric role
CASP206hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_idMCSA4
Number of Residues2
DetailsM-CSA 306
ChainResidueDetails
DASP105hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, steric role
DASP206hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon