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Crystal structure of the AWP1 (adhesin-like wall protein 1) a-domain from candida glabrata

Analyse Crystal structure of the AWP1 (adhesin-like wall protein 1) a-domain from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7O9Q
Type: protein
Length: 615 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: AWP1A
UniProt: Q6FPN0
Ligands: 9JE
Pockets: 1 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 1% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	AWP1A	protein	307	1% helix, 53% strand	Q6FPN0
B	AWP1A	protein	308	1% helix, 53% strand	Q6FPN0

Ligands and binding sites

9JE · pentane-1,5-diol · ligand · 4 copies · chains A, B

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1159	0.77	0.79	127	empty

Interfaces

1 interface between chains.

A–B · 695 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

7O9Q · Crystal structure of the Awp1 (adhesin-like wall protein 1) A-domain from Candida glabrata · the same entry in another collection · chain A against A, TM-score 1.00

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 Q6FPN0
Elsewhere: RCSB PDB 7O9Q · PDBe 7O9Q · UniProt Q6FPN0

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