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Crystal structure of the P450 domain of the CYP51-ferredoxin fusion protein from methylococcus capsulatus, ligand-free state

Analyse Crystal structure of the P450 domain of the CYP51-ferredoxin fusion protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6MI0
Type: protein
Length: 446 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome P450 51
EC: 1.14.13.70
UniProt: Q603T8
Ligands: HEM
Pockets: 4 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome P450 51 (EC 1.14.13.70)	protein	446	52% helix, 11% strand	Q603T8

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	1100	0.84	0.84	79	HEM
2	121	0.40	0.75	22	empty
3	87	0.36	0.75	18	empty
4	65	0.29	0.74	14	empty

Compared structures

6MI0 · Crystal structure of the P450 domain of the CYP51-ferredoxin fusion protein from… · 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 Q603T8
Elsewhere: RCSB PDB 6MI0 · PDBe 6MI0 · UniProt Q603T8

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