MolNFT v1 · #52013 · protein

Thioredoxin a active site mutants form mixed disulfide dimers that resemble enzyme-substrate reaction intermediate

2VOC: “Thioredoxin a active site mutants form mixed disulfide dimers that resemble enzyme-substrate reaction…”. X-ray diffraction. MolNFT v1 #52013 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2VOC
Type: protein
Length: 214 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thioredoxin
UniProt: P14949

Structure

x-ray diffraction · 2 distinct chains · 33% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thioredoxin	protein	110	32% helix, 27% strand	P14949
B	Thioredoxin	protein	104	34% helix, 29% strand	P14949

Ligands and binding sites

PEG · Di(hydroxyethyl)ether · additive · chains A

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

Interfaces

1 interface between chains.

A–B · 477 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

2VOC · Thioredoxin a active site mutants form mixed disulfide dimers that resemble… · the same entry in another collection · chain A against A, TM-score 1.00
P14949 · AlphaFold monomer V2.0 prediction for thioredoxin (P14949) · a predicted model of the same protein · chain B against A, TM-score 0.95

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 P14949
Elsewhere: RCSB PDB 2VOC · PDBe 2VOC · UniProt P14949

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