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Crystal structure of cytochrome P450 CYP267B1 from sorangium cellulosum so CE56

Analyse Crystal structure of cytochrome P450 CYP267B1 from sorangium cellulosum so CE56 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6GK5
Type: protein
Length: 403 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome P450 CYP267B1 protein
EC: 1.14.-.-
UniProt: A9ERX9
Ligands: HEM
Pockets: 4 · best druggability 0.87

Structure

x-ray diffraction · 1 distinct chain · 56% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome P450 CYP267B1 protein (EC 1.14.-.-)	protein	403	56% helix, 8% strand	A9ERX9

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1026	0.87	0.88	92	HEM
2	70	0.41	0.80	18	empty
3	113	0.40	0.75	20	empty
4	52	0.33	0.78	17	empty

Compared structures

6GK5 · Crystal structure of cytochrome P450 CYP267B1 from Sorangium cellulosum So ce56 · the same entry in another collection · chain A against A, TM-score 1.00

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 A9ERX9
Elsewhere: RCSB PDB 6GK5 · PDBe 6GK5 · UniProt A9ERX9

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