Research workbench

Collagen adhesin and collagen complex structure

Analyse Collagen adhesin and collagen complex structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2F6A
Type: protein
Length: 1,378 residues
Chains: 10
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Collagen adhesin; Collagen
UniProt: Q53654
Pockets: 14 · best druggability 0.75

Structure

x-ray diffraction · 4 distinct chains · 6% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Collagen adhesin	protein	303	7% helix, 58% strand	Q53654
B, C, D	Collagen adhesin	protein	299	6% helix, 57% strand	Q53654
E, F, G, H, I	Collagen	protein	30	0% helix, 3% strand	—
J	Collagen	protein	28	0% helix, 0% strand	—

Pockets

14 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	988	0.75	0.78	96	empty
2	888	0.75	0.79	103	empty
3	278	0.65	0.82	46	empty
4	257	0.62	0.81	26	empty
5	89	0.44	0.80	19	empty

Interfaces

25 interfaces between chains.

F–G · 929 Å² buried · 10 hydrogen bonds · protein-protein
E–F · 916 Å² buried · 10 hydrogen bonds · protein-protein
H–I · 871 Å² buried · 7 hydrogen bonds · protein-protein
E–G · 835 Å² buried · 12 hydrogen bonds · protein-protein
H–J · 820 Å² buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 47 modified (hydroxylation).

Compared structures

2F6A · Collagen Adhesin and Collagen Complex Structure · the same entry in another collection · chain J against J, TM-score 1.00
Q53654 · AlphaFold monomer V2.0 prediction for collagen adhesin (Q53654) · 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 Q53654
Elsewhere: RCSB PDB 2F6A · PDBe 2F6A · UniProt Q53654

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