MolNFT v1 · #33425 · protein

Structure of core-swapped mutant of fibronectin

2CK2 · Human fibronectin: “Structure of core-swapped mutant of fibronectin”. X-ray diffraction, 1 ligand (ACE), 2 pockets (best druggability 0.45). MolNFT v1 #33425 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2CK2
Type: protein
Length: 190 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Human fibronectin
UniProt: P02751
Ligands: ACE
Pockets: 2 · best druggability 0.45

Structure

x-ray diffraction · 2 distinct chains · 0% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Human fibronectin	protein	94	0% helix, 53% strand	P02751
B	Human fibronectin	protein	96	0% helix, 52% strand	P02751

Ligands and binding sites

ACE · Acetyl group · ligand · 2 copies · chains A, B

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	68	0.45	0.83	18	empty
2	160	0.41	0.73	22	empty

Interfaces

1 interface between chains.

A–B · 542 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

2CK2 · Structure of core-swapped mutant of fibronectin · the same entry in another collection · chain A against A, TM-score 1.00
P02751 · AlphaFold monomer V2.0 prediction for fibronectin (P02751) · a predicted model of the same protein · chain A against A, TM-score 0.90

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 P02751
Elsewhere: RCSB PDB 2CK2 · PDBe 2CK2 · UniProt P02751

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