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Crystal structure of the cytochrome P450 CYP121 S279A mutant from M. tuberculosis

Analyse Crystal structure of the cytochrome P450 CYP121 S279A mutant from M.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3CY1
Type: protein
Length: 394 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome P450 121
EC: 1.14.-.-
UniProt: P0A514
Ligands: HEM, SO4
Pockets: 3 · best druggability 0.87

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome P450 121 (EC 1.14.-.-)	protein	394	51% helix, 10% strand	P0A514

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
SO4 · Sulfate ion · ion · 3 copies · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	826	0.87	0.89	78	HEM
2	52	0.41	0.82	19	empty
3	59	0.40	0.81	18	empty

Compared structures

3CY1 · Crystal structure of the cytochrome P450 CYP121 S279A mutant from M. tuberculosis · 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 P0A514
Elsewhere: RCSB PDB 3CY1 · PDBe 3CY1 · UniProt P0A514

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