MolNFT v1 · #2780 · protein

0.97 a "ab initio" crystal structure of cytochrome C-553 from bacillus pasteurii

1C75: “0.97 a "ab initio" crystal structure of cytochrome C-553 from bacillus pasteurii”. X-ray diffraction, 1 ligand (HEC), 1 pocket (best druggability 0.58). MolNFT v1 #2780 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1C75
Type: protein
Length: 71 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome C-553
UniProt: P82599
Ligands: HEC
Pockets: 1 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome C-553	protein	71	52% helix, 3% strand	P82599

Ligands and binding sites

HEC · Heme C · ligand · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	152	0.58	0.82	23	HEC

Modifications

Observed in the structure: 2 cofactor (heme c attachment).

Compared structures

1C75 · 0.97 a "ab initio" crystal structure of cytochrome C-553 from bacillus pasteurii · the same entry in another collection · chain A against A, TM-score 1.00
P82599 · AlphaFold monomer V2.0 prediction for cytochrome C-553 (P82599) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P82599
Elsewhere: RCSB PDB 1C75 · PDBe 1C75 · UniProt P82599

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