MolNFT v1 · #3361 · protein

Crystal structure and refinement of cytochrome P450-terp at 2.3 ångströms resolution

1CPT: “Crystal structure and refinement of cytochrome P450-terp at 2.3 ångströms resolution”. X-ray diffraction, 1 ligand (HEM), 4 pockets (best druggability 0.83). MolNFT v1 #3361 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 1CPT
Type: protein
Length: 412 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome P450-terp
UniProt: P33006
Ligands: HEM
Pockets: 4 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome P450-terp	protein	412	53% helix, 12% strand	P33006

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	803	0.83	0.86	89	HEM
2	59	0.47	0.85	17	empty
3	70	0.33	0.75	16	empty
4	50	0.25	0.73	13	empty

Compared structures

1CPT · Crystal structure and refinement of cytochrome P450-terp at 2.3 ångströms resolution · the same entry in another collection · chain A against A, TM-score 1.00
P33006 · AlphaFold monomer V2.0 prediction for cytochrome P450-terp (P33006) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P33006
Elsewhere: RCSB PDB 1CPT · PDBe 1CPT · UniProt P33006

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