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Crystal structure of a catalytic site mutant E. COLI trxa (caca)

Analyse Crystal structure of a catalytic site mutant E. COLI trxa (caca) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ZCP
Type: protein
Length: 424 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thioredoxin 1
UniProt: P0AA25
Pockets: 3 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Thioredoxin 1	protein	106	31% helix, 28% strand	P0AA25

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	372	0.56	0.74	40	empty
2	110	0.54	0.83	22	empty
3	129	0.53	0.81	25	empty

Interfaces

3 interfaces between chains.

C–D · 389 Å² buried · 5 hydrogen bonds · protein-protein
A–B · 379 Å² buried · 6 hydrogen bonds · protein-protein
A–C · 178 Å² buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

1ZCP · Crystal Structure of a catalytic site mutant E. coli TrxA (CACA) · the same entry in another collection · chain A against A, TM-score 1.00
P0AA25 · AlphaFold monomer V2.0 prediction for thioredoxin 1 (P0AA25) · 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 P0AA25
Elsewhere: RCSB PDB 1ZCP · PDBe 1ZCP · UniProt P0AA25

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