Structure of PDB 4jo0 Chain A

Receptor sequence
>4jo0A (length=522) Species: 54571 (Streptomyces venezuelae) [Search protein sequence]
SHMRYSLRQDIAVEPVIAGWYGWSYLLPPQTLARFVHNRFNRIVESYLDD
PQVHAAAVRQRRMHGGPWIHAHEHRDAIEAWYRETAPRRERLDELFEAVR
RLEEDILPRHHGECLDPVYQELPAALAGRVEVFYGRDNRTADYRFVEPLM
YASEYYDESWQQVRFRPVTEDAREFALTTPMLEYGPEQLLVNVPLNSPLL
DAVFRGGLTGTELDDLAARFGLDGERAARFASYFEPTPEEDVLEYVGHAC
VFARHRGTTFLVDPVLSYSGYPGGAENRFTFADLPERIDHLLITHNHQDH
MLFETLLRIRHRVGRVLVPKSTNASLVDPGLGGILRRLGFTDVVEVDDLE
TLSCGSAEVVALPFLGEHGDLRIRSKTGWLIRFGERSVLFAADSTNISPT
MYTKVAEVIGPVDTVFIGMESIGAAASWIYGPLYGEPLDRRTDQSRRLNG
SNFPQAREIVDALEPDEVYVYAMGLEPWMGVVMAVDYDESHPAIVDSDLL
VRHVQDKGGTAERLHLRRTLRL
3D structure
PDB4jo0 Structure of a Dinuclear Iron Cluster-Containing beta-Hydroxylase Active in Antibiotic Biosynthesis.
ChainA
Resolution2.17 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.14.99.65: 4-amino-L-phenylalanyl-[CmlP-peptidyl-carrier-protein] 3-hydroxylase.
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 H305 H307 E377 D403 H295 H297 E367 D393
BS02 FE A D309 H310 D403 D299 H300 D393
BS03 O A H307 D309 H310 D403 H297 D299 H300 D393
BS04 ACT A H258 D309 D403 E430 A482 H248 D299 D393 E420 A472
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
Biological Process
GO:0017000 antibiotic biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4jo0, PDBe:4jo0, PDBj:4jo0
PDBsum4jo0
PubMed23980641
UniProtF2RB80|CMLA_STRVP 4-amino-L-phenylalanyl-[CmlP-peptidyl-carrier-protein] 3-hydroxylase (Gene Name=cmlA)

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