Structure of PDB 1kgp Chain A

Receptor sequence
>1kgpA (length=296) Species: 1697 (Corynebacterium ammoniagenes) [Search protein sequence]
SNEYDEYIANHTDPVKAINWNVIPDEKDLEVWDRLTGNFWLPEKIPVSND
IQSWNKMTPQEQLATMRVFTGLTLLDTIQGTVGAISLLPDAETMHEEAVY
TNIAFMESVHAKSYSNIFMTLASTPQINEAFRWSEENENLQRKAKIIMSY
YNGDDPLKKKVASTLLESFLFYSGFYLPMYLSSRAKLTNTADIIRLIIRD
ESVHGYYIGYKYQQGVKKLSEAEQEEYKAYTFDLMYDLYENEIEYTEDIY
DDLGWTEDVKRFLRYNANKALNNLGYEGLFPTDETKVSPAILSSLS
3D structure
PDB1kgp Crystal structure of the di-iron/radical protein of ribonucleotide reductase from Corynebacterium ammoniagenes.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y115 D201
Catalytic site (residue number reindexed from 1) Y114 D200
Enzyme Commision number 1.17.4.1: ribonucleoside-diphosphate reductase.
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 MN A D77 E108 H111 F172 E202 D76 E107 H110 F171 E201
BS02 MN A E108 E168 E202 H205 E107 E167 E201 H204
Gene Ontology
Molecular Function
GO:0004748 ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
Biological Process
GO:0009263 deoxyribonucleotide biosynthetic process
Cellular Component
GO:0005971 ribonucleoside-diphosphate reductase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1kgp, PDBe:1kgp, PDBj:1kgp
PDBsum1kgp
PubMed11802741
UniProtO69274

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