Structure of PDB 2vck Chain B

Receptor sequence
>2vckB (length=209) Species: 268746 (Prochlorococcus phage P-SSM2) [Search protein sequence]
KTIWQNYIDALFETFPQLEISEVWAKWDGGNVGDAKLTANIRTGEHFLKA
REAHIVDPNSDIYNTILYPKTGADLPCFGMDLMKFSDKKVIIVFDFQHPR
EKYLFSVDGLPEDDGKYRFFEMGNHFSKNIFVRYCKPDEVDQYLDTFKLY
LTKYKEMIDNNKPVGEDTTVYSDFDTYMTELDPVRGYMKNKFGEGRSEAF
VNDFLFSYK
3D structure
PDB2vck Phycoerythrobilin Synthase (Pebs) of a Marine Virus: Crystal Structures of the Biliverdin Complex and the Substrate-Free Form.
ChainB
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D105 D206
Catalytic site (residue number reindexed from 1) D81 D182
Enzyme Commision number 1.3.7.6: phycoerythrobilin 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 BLA B I86 N88 I90 D105 M107 I115 V117 Y141 R142 F143 F144 Y158 M202 D206 P207 V208 Y211 I62 N64 I66 D81 M83 I91 V93 Y117 R118 F119 F120 Y134 M178 D182 P183 V184 Y187
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0016636 oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor
GO:0050897 cobalt ion binding
Biological Process
GO:0010024 phytochromobilin biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2vck, PDBe:2vck, PDBj:2vck
PDBsum2vck
PubMed18662988
UniProtQ58MU6|PEBS_BPPRM Phycoerythrobilin synthase (Gene Name=pebS)

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