MolNFT v1 · #52337 · protein

The fourth FAS1 domain structure of human BIGH3

2VXP · Transforming growth factor-beta-induced protein ig-H3: “The fourth FAS1 domain structure of human BIGH3”. X-ray diffraction. MolNFT v1 #52337 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2VXP
Type: protein
Length: 262 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transforming growth factor-beta-induced protein ig-H3
UniProt: Q15582

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Transforming growth factor-beta-induced protein ig-H3	protein	131	34% helix, 30% strand	Q15582

Interfaces

1 interface between chains.

A–B · 17 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

2VXP · The fourth FAS1 domain structure of human Bigh3 · the same entry in another collection · chain A against A, TM-score 1.00
Q15582 · AlphaFold monomer V2.0 prediction for transforming growth factor- beta-induced protein… · a predicted model of the same protein · chain B against A, TM-score 0.97

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 Q15582
Elsewhere: RCSB PDB 2VXP · PDBe 2VXP · UniProt Q15582

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