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2X9J

Structure of the Mutant D206N of Phycoerythrobilin Synthase PebS from the Cyanophage P-SSM2 in complex with 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
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE BLA A 1234
ChainResidue
AILE79
ATYR141
AARG142
APHE143
APHE144
ATYR158
AMET202
AASN206
APRO207
AVAL208
ATYR211
AILE86
AHOH2218
AHOH2219
AASN88
AILE90
AASP105
AMET107
AILE115
AVAL117
AGLN121

site_idAC2
Number of Residues23
DetailsBINDING SITE FOR RESIDUE BLA B 1234
ChainResidue
BILE79
BILE86
BASN88
BILE90
BASP105
BMET107
BILE115
BVAL117
BGLN121
BTYR141
BARG142
BPHE143
BPHE144
BPHE150
BTYR158
BMET202
BASN206
BPRO207
BVAL208
BTYR211
BPHE230
BHOH2209
BHOH2210

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
AASN206hydrogen 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
BASN206hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

221051

PDB entries from 2024-06-12

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