Structure of PDB 1w2n Chain A

Receptor sequence
>1w2nA (length=277) Species: 1901 (Streptomyces clavuligerus) [Search protein sequence]
MDTTVPTFSLAELQQGLHQDEFRRCLRDKGLFYLTDCGLTDTELKSAKDL
VIDFFEHGSEAEKRAVTSPVPTMRRGFTGLESYSMCYSMGTADNLFPSGD
FERIWTQYFDRQYTASRAVAREVLRATGTEPDGGVEAFLDCEPLLRFRYF
PQVPEPLRMAPHYDLSMVTLIQQTPCANGFVSLQAEVGGAFTDLPYRPDA
VLVFCGAIATLVTGGQVKAPRHHVAAPRRDQIAGSSRTSSVFFLRPNADF
TFSVPLARECGFDVSLDGETATFQDWI
3D structure
PDB1w2n Conformational Flexibility of the C Terminus with Implications for Substrate Binding and Catalysis Revealed in a New Crystal Form of Deacetoxycephalosporin C Synthase
ChainA
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 FE A H183 D185 H243 H162 D164 H222
BS02 PN1 A R160 R162 H183 L186 R146 R148 H162 L165
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1w2n, PDBe:1w2n, PDBj:1w2n
PDBsum1w2n
PubMed15381427
UniProtP18548|CEFE_STRCL Deacetoxycephalosporin C synthase (Gene Name=cefE)

[Back to BioLiP]