Structure of PDB 5vws Chain A

Receptor sequence
>5vwsA (length=376) Species: 469371 (Thermobispora bispora DSM 43833) [Search protein sequence]
GQPSLTDGGAALFAWLRTMRNEHPVWRDQFGIYHVFRYDDVRQILGDYQT
FSSDRTRLGKGGITMIDPPEHRHQRRLITHAFTPQSISAMEPRIRQIADH
LLDELPGPEFDLVEHFAYPLPVIVIAELLGVPPGDRHLFRTWSDRLMSLQ
VEADPELARTVAAAMTEMNDYLREHCRSRRTHPRDDLLTRLVQAEVEGKR
LDLEEVVNTASLLLLAGHLTTTVLIGNTMLCLWDHPEAEKAVRADPSLIP
AALEESLRLRSPFLQAGRVTTRDVTIAGETIPANRFVMAWILSANHDDRR
FPDPERFDLHRQTTGHIAFGHGVHFCLGAQLGRLEGRIALERLLGRFTEI
HPWPREGISFYQSAIFGASRMPVRCG
3D structure
PDB5vws P450-Mediated Non-natural Cyclopropanation of Dehydroalanine-Containing Thiopeptides.
ChainA
Resolution2.411 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S160 A230 L233 T234 T235 C340 L341 G342 E349 I379
Catalytic site (residue number reindexed from 1) S148 A216 L219 T220 T221 C326 L327 G328 E335 I365
Enzyme Commision number ?
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 HEM A I75 T76 H83 R87 A230 G231 T234 L238 P276 R282 F333 H338 C340 G342 I63 T64 H71 R75 A216 G217 T220 L224 P262 R268 F319 H324 C326 G328
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0020037 heme binding
GO:0046872 metal ion binding

View graph for
Molecular Function
External links
PDB RCSB:5vws, PDBe:5vws, PDBj:5vws
PDBsum5vws
PubMed28535034
UniProtD6Y4Z8

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