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Thermus thermophilus cytochrome C552 synthesized by escherichia COLI

Analyse Thermus thermophilus cytochrome C552 synthesized by escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1DT1
Type: protein
Length: 129 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome C552
UniProt: Q5SME3
Ligands: HEC
Pockets: 1 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome C552	protein	129	49% helix, 9% strand	Q5SME3

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	212	0.75	0.89	35	HEC

Modifications

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

Compared structures

1DT1 · Thermus thermophilus cytochrome C552 synthesized by escherichia COLI · the same entry in another collection · chain A against A, TM-score 1.00
Q5SME3 · AlphaFold monomer V2.0 prediction for cytochrome C-552 (Q5SME3) · 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 Q5SME3
Elsewhere: RCSB PDB 1DT1 · PDBe 1DT1 · UniProt Q5SME3

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