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Cyt P460 of nitrosomonas sp. AL212

Analyse Cyt P460 of nitrosomonas sp. AL212 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6AMG
Type: protein
Length: 318 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome P460
UniProt: F9ZFJ0
Ligands: HEC
Pockets: 4 · best druggability 0.67

Structure

x-ray diffraction · 2 distinct chains · 23% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome P460	protein	158	24% helix, 36% strand	F9ZFJ0
B	Cytochrome P460	protein	160	22% helix, 36% strand	F9ZFJ0

Ligands and binding sites

HEC · Heme C · ligand · 2 copies · chains A, B

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

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	214	0.67	0.85	35	HEC
2	205	0.66	0.84	36	HEC
3	56	0.29	0.74	15	empty
4	59	0.27	0.73	14	empty

Interfaces

1 interface between chains.

A–B · 1642 Å² buried · 20 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 cofactor (heme c attachment).

Compared structures

6AMG · cyt P460 of Nitrosomonas sp. AL212 · 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 F9ZFJ0
Elsewhere: RCSB PDB 6AMG · PDBe 6AMG · UniProt F9ZFJ0

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