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Structural and functional characterizations of a thioredoxin-fold protein from helicobacter pylori

Analyse Structural and functional characterizations of a thioredoxin-fold protein from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4FYC
Type: protein
Length: 323 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: THIOL:DISULFIDE interchange protein (dsbc)
UniProt: O25140
Pockets: 1 · best druggability 0.70

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	THIOL:DISULFIDE interchange protein (dsbc)	protein	162	41% helix, 25% strand	O25140
B	THIOL:DISULFIDE interchange protein (dsbc)	protein	161	37% helix, 24% strand	O25140

Ligands and binding sites

PG4 · Tetraethylene glycol · additive · 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	720	0.70	0.78	65	empty

Interfaces

1 interface between chains.

A–B · 320 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

4FYC · Structural and functional characterizations of a thioredoxin-fold protein from… · 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 O25140
Elsewhere: RCSB PDB 4FYC · PDBe 4FYC · UniProt O25140

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