MolNFT v1 · #23466 · protein

Crystal structure analysis of the C37L/C151T/C442A-triple mutant of CYP51 from mycobacterium tuberculosis

1U13 · Cytochrome P450 51: “Crystal structure analysis of the C37L/C151T/C442A-triple mutant of CYP51 from mycobacterium tuberculosis”. X-ray diffraction, 1 ligand (HEM), 5 pockets (best druggability 0.80). MolNFT v1 #23466 on GenesisL1…

PDB: 1U13
Type: protein
Length: 433 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: P0A512
Ligands: HEM
Pockets: 5 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome P450 51 (EC 1.14.13.70)	protein	433	55% helix, 12% strand	P0A512

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

5 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	689	0.80	0.84	62	HEM
2	83	0.38	0.77	19	empty
3	50	0.35	0.79	14	empty
4	79	0.33	0.74	19	empty
5	63	0.32	0.75	16	empty

Compared structures

1U13 · Crystal structure analysis of the C37L/C151T/C442A-triple mutant of CYP51 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 P0A512
Elsewhere: RCSB PDB 1U13 · PDBe 1U13 · UniProt P0A512

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