Structure of PDB 2jjo Chain A

Receptor sequence

>2jjoA (length=393) Species: 1836 (Saccharopolyspora erythraea) [Search protein sequence]

DEVPGMADETALLDWLGTMREKQPVWQDRYGVWHVFRHADVQTVLRDTAT
FSSDPTRVIEGASPTPGMIHEIDPPEHRALRKVVSSAFTPRTISDLEPRI
RDVTRSLLADAGESFDLVDVLAFPLPVTIVAELLGLPPMDHEQFGDWSGA
LVDIQMDDPTDPALAERIADVLNPLTAYLKARCAERRADPGDDLISRLVL
AEVDGRALDDEEAANFSTALLLAGHITTTVLLGNIVRTLDEHPAHWDAAA
EDPGRIPAIVEEVLRYRPPFPQMQRTTTKATEVAGVPIPADVMVNTWVLS
ANRDSDAHDDPDRFDPSRKSGGAAQLSFGHGVHFCLGAPLARLENRVALE
EIIARFGRLTVDRDDERLRHFEQIVLGTRHLPVLAGSSPRQSA

3D structure

PDB

2jjo Investigating the Structural Plasticity of a Cytochrome P450: Three-Dimensional Structures of P450 Eryk and Binding to its Physiological Substrate.

Chain

Resolution

1.99 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	D171 A241 I244 T245 T246 C353 L354 G355 E362 V393
Catalytic site (residue number reindexed from 1)	D153 A223 I226 T227 T228 C335 L336 G337 E344 V375
Enzyme Commision number	1.14.13.154: erythromycin 12 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	HEM	A	H95 R99 F106 L238 A241 G242 T245 T246 L249 M291 R293 S345 F346 H351 C353 L354 G355 A359	H77 R81 F88 L220 A223 G224 T227 T228 L231 M273 R275 S327 F328 H333 C335 L336 G337 A341
BS02	EY5	A	H88 E89 L169 M174 I186 A237 A241 T245 F288 Q292	H70 E71 L151 M156 I168 A219 A223 T227 F270 Q274	MOAD: Kd=3.5uM

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:0016709	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen
GO:0020037	heme binding
GO:0046872	metal ion binding
GO:0050661	NADP binding

	Biological Process
GO:0017000	antibiotic biosynthetic process
GO:0033068	macrolide biosynthetic process

View graph for
Molecular Function

View graph for
Biological Process

External links

PDB	RCSB:2jjo, PDBe:2jjo, PDBj:2jjo
PDBsum	2jjo
PubMed	19625248
UniProt	P48635\|ERYK_SACEN Erythromycin C-12 hydroxylase (Gene Name=eryK)

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