Structure of PDB 5kil Chain A

Receptor sequence
>5kilA (length=510) Species: 953739 (Streptomyces venezuelae ATCC 10712) [Search protein sequence]
RYSLRQDIAVEPVIAGWYGWSYLLPPQTLARFVHNRFNRIVESYLDDPQV
HAAAVRQRRMHGGPWIHAHEHRDAIEAWYRETAPRRERLDELFEAVRRLE
EDILPRHHGECLDPVYQELPAALAGRVEVFYGRDNRTADYRFVEPLMYAS
EYYDESWQQVRFRPVTEDAREFALTTPMLEYGPEQLLVNVPLNSPLLDAV
FRGGLTGTELDDLAARFGLDGERAARFASYFEPTPEDVLEYVGHACVFAR
HRGTTFLVDPVLSYSGYPGGAENRFTFADLPERIDHLLITHNHQDHMLFE
TLLRIRHRVGRVLVPKSTNASLVDPGLGGILRRLGFTDVVEVDDLETLSC
GSAEVVALPFLGDHGDLRIRSKTGWLIRFGERSVLFAADSTNISPTMYTK
VAEVIGPVDTVFIGMESIGAAASWIYGPLYGEPLDRRTDQSRRLNGSNFP
QAREIVDALEPDEVYVYAMGLEPWMGVVMPAIVDSDLLVRHVQDKGGTAE
RLHLRRTLRL
3D structure
PDB5kil A Carboxylate Shift Regulates Dioxygen Activation by the Diiron Nonheme beta-Hydroxylase CmlA upon Binding of a Substrate-Loaded Nonribosomal Peptide Synthetase.
ChainA
Resolution2.72 Å
3D
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
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 FEO A H305 H307 D309 H310 D377 D403 H291 H293 D295 H296 D363 D389
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5kil, PDBe:5kil, PDBj:5kil
PDBsum5kil
PubMed27668828
UniProtF2RB80|CMLA_STRVP 4-amino-L-phenylalanyl-[CmlP-peptidyl-carrier-protein] 3-hydroxylase (Gene Name=cmlA)

[Back to BioLiP]