MolNFT v1 · #84436 · protein

Structure of a mutant of P450 eryk in complex with erythromycin B.

3ZKP · Erythromycin C-12 hydroxylase: “Structure of a mutant of P450 eryk in complex with erythromycin B.”. X-ray diffraction, 2 ligands (HEM, ERB), 3 pockets (best druggability 0.85). MolNFT v1 #84436 on GenesisL1: 3D structure, binding…

PDB: 3ZKP
Type: protein
Length: 391 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Erythromycin C-12 hydroxylase
EC: 1.14.13.154
UniProt: P48635
Ligands: HEM, ERB
Pockets: 3 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Erythromycin C-12 hydroxylase (EC 1.14.13.154)	protein	391	53% helix, 11% strand	P48635

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
ERB · Erythromycin B · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1142	0.85	0.85	86	HEM, ERB
2	128	0.52	0.81	18	empty
3	82	0.36	0.76	20	empty

Compared structures

3ZKP · Structure of a mutant of P450 EryK in complex with erythromycin B. · the same entry in another collection · chain A against A, TM-score 1.00
P48635 · AlphaFold monomer V2.0 prediction for erythromycin C-12 hydroxylase (P48635) · a predicted model of the same protein · chain A against A, TM-score 0.96

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P48635
Elsewhere: RCSB PDB 3ZKP · PDBe 3ZKP · UniProt P48635

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