MolNFT v1 · #130212 · protein

AlphaFold monomer V2.0 prediction for fibrinogen beta chain (P02676)

P02676: “AlphaFold monomer V2.0 prediction for fibrinogen beta chain (P02676)”. MolNFT v1 #130212 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

Accession: P02676
Type: protein
Length: 468 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x88DB42AFD1c918761d553B3c6CEc7ba83c6f79bC
UniProt: P02676

Structure

1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	468	—	P02676

Compared structures

1DEQ · The crystal structure of modified bovine fibrinogen (at ~4 ångström resolution) · an experimental structure of the same protein · chain A against E, TM-score 0.78
1DEQ · The crystal structure of modified bovine fibrinogen (at ~4 ångström resolution) · an experimental structure of the same protein · chain A against E, TM-score 0.78
1JY2 · Crystal structure of the central region of bovine fibrinogen (E5 fragment) at 1.4… · an experimental structure of the same protein · chain A against O, TM-score 0.10
1JY2 · Crystal Structure of the Central Region of Bovine Fibrinogen (E5 fragment) at 1.4… · an experimental structure of the same protein · chain A against O, TM-score 0.10
1JY3 · Crystal Structure of the Central Region of Bovine Fibrinogen (E5 Fragment) at 1.4… · an experimental structure of the same protein · chain A against O, TM-score 0.10
1JY3 · Crystal structure of the central region of bovine fibrinogen (E5 fragment) at 1.4… · an experimental structure of the same protein · chain A against O, TM-score 0.10

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 P02676
Elsewhere: UniProt P02676 · AlphaFold DB P02676

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