Structure of PDB 3kp1 Chain C

Receptor sequence
>3kp1C (length=726) Species: 1511 (Acetoanaerobium sticklandii) [Search protein sequence]
LRVNEKLDVENILKDLDKYTPKRRGWTWRQPAENLQMGPFIYKDASTPLE
NSVALPSAKYFGDIDPQPLPVITTEIASGRFEDDIRRMRMAAWHGADHIM
VIRTAGQSHYDGLIEGTPQGIGGVPITRKQVRAQRKALDLIEEEVGRPIN
YHSYVSGVAGPDIAVMFAEEGVNGAHQDPQYNVLYRNINMIRSFIDACES
KTIMAWADMAQIDGAHNANATAREAWKVMPELMVQHALNSIFSLKVGMKK
SNICLSTVPPTAPPAPSMYLDLPYAVALREMFEGYRMRAQMNTKYMEAST
REATVTHVLNLLISKLTRADIQSTITPDEGRNVPWHIYNIEACDTAKQAL
IGMDGLMDMVQLKREGVLGDTVRELKERAVLFMEEIIEAGGYFNAVEQGF
FVDSGYYPERNGDGIARQINGGIGAGTVFERDEDYMAPVTAHFGYNNVKQ
YDEALVSEPSKLIDGCTLEVPEKIVYIDELDENDNVNVRMEETKEFRSMI
KPEVEWQADGTVLLTMFLPTSKRVAEFAAIEFAKKMNLEEVEVINREVMQ
EAEGTRIELKGRVPFSIDINSLVIPPILSEDEIREDIEKTPLKIVAATVG
EDEHSVGLREVIDIKHGGIEKYGVEVHYLGTSVPVEKLVDAAIELKADAI
LASTIISHDDIHYKNMKRIHELAVEKGIRDKIMIGCGGTQVTPEVAVKQG
VDAGFGRGSKGIHVATFLVKKRREMR
3D structure
PDB3kp1 Large-scale domain dynamics and adenosylcobalamin reorientation orchestrate radical catalysis in ornithine 4,5-aminomutase.
ChainC
Resolution2.01 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y187 H225 R297 K629
Catalytic site (residue number reindexed from 1) Y181 H216 R288 K615
Enzyme Commision number 5.4.3.5: D-ornithine 4,5-aminomutase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016853 isomerase activity
GO:0031419 cobalamin binding
GO:0046872 metal ion binding
GO:0046983 protein dimerization activity
GO:0047831 D-ornithine 4,5-aminomutase activity

View graph for
Molecular Function
External links
PDB RCSB:3kp1, PDBe:3kp1, PDBj:3kp1
PDBsum3kp1
PubMed20106986
UniProtE3PY95|OAME_ACESD D-ornithine 4,5-aminomutase subunit beta (Gene Name=oraE)

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