Structure of PDB 1hjf Chain A

Receptor sequence
>1hjfA (length=273) Species: 1901 (Streptomyces clavuligerus) [Search protein sequence]
MDTTVPTFSLAELQQGLHQDEFRRCLRDKGLFYLTDCGLTDTELKSAKDI
VIDFFEHGSEAEKRAVTSPVPTMRRGFTGLETGSYSDYSMCYSMGTADNL
FPSGDFERIWTQYFDRQYTASRAVAREVLRATGTEPDGGVEAFLDCEPLL
RFRYFLRMAPHYDLSMVTLIQQTFVSLQAEVGGAFTDLPYRPDAVLVFCG
AIATLVTGGQVKAPRHHVAASQTSSVFFLRPNADFTFSVPLARECGFDVS
LDGETATFQDWIGGNYVNIRRTS
3D structure
PDB1hjf Alteration of the 2-Oxoacid Cosubstrate Selectivity in Deacetoxycephalosporin C Synthase: The Role of Arginine-258
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R74
Catalytic site (residue number reindexed from 1) R74
Enzyme Commision number 1.14.20.1: deacetoxycephalosporin-C 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 FE2 A H183 D185 H243 T308 S309 H161 D163 H216 T272 S273
BS02 COI A M180 H183 I192 H243 M158 H161 I170 H216
Gene Ontology
Molecular Function
GO:0005506 iron ion binding
GO:0016491 oxidoreductase activity
GO:0016706 2-oxoglutarate-dependent dioxygenase activity
GO:0031418 L-ascorbic acid binding
GO:0050599 deacetoxycephalosporin-C synthase activity
Biological Process
GO:0009058 biosynthetic process
GO:0017000 antibiotic biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1hjf, PDBe:1hjf, PDBj:1hjf
PDBsum1hjf
PubMed11279000
UniProtP18548|CEFE_STRCL Deacetoxycephalosporin C synthase (Gene Name=cefE)

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