MolNFT v1 · #2711 · protein

Thermus thermophilus cytochrome-C552: a new highly thermostable cytochrome-C structure obtained by mad phasing

1C52: “Thermus thermophilus cytochrome-C552: a new highly thermostable cytochrome-C structure obtained by mad phasing”. X-ray diffraction, 1 ligand (HEM), 1 pocket (best druggability 0.75). MolNFT v1 #2711 on GenesisL1: 3D structure…

PDB: 1C52
Type: protein
Length: 131 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome-C552
UniProt: P04164
Ligands: HEM
Pockets: 1 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome-C552	protein	131	46% helix, 12% strand	P04164

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

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	215	0.75	0.89	35	HEM

Modifications

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

Compared structures

1C52 · Thermus thermophilus cytochrome-C552: a new highly thermostable cytochrome-C structure… · the same entry in another collection · chain A against A, TM-score 1.00
P04164 · AlphaFold monomer V2.0 prediction for cytochrome C-552 (P04164) · 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 P04164
Elsewhere: RCSB PDB 1C52 · PDBe 1C52 · UniProt P04164

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