MolNFT v1 · #92022 · protein

Structural basis for ZN2+-dependent intercellular adhesion in staphylococcal biofilms

4FUP · Accumulation associated protein: “Structural basis for ZN2+-dependent intercellular adhesion in staphylococcal biofilms”. X-ray diffraction, 1 ligand (ZN), 1 pocket (best druggability 0.44). MolNFT v1 #92022 on GenesisL1: 3D…

PDB: 4FUP
Type: protein
Length: 394 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Accumulation associated protein
UniProt: Q5HKE8
Ligands: ZN
Pockets: 1 · best druggability 0.44

Structure

x-ray diffraction · 2 distinct chains · 0% helix, 56% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Accumulation associated protein	protein	199	0% helix, 56% strand	Q5HKE8
B	Accumulation associated protein	protein	195	0% helix, 55% strand	Q5HKE8

Ligands and binding sites

ZN · Zinc ion · metal · 2 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	122	0.44	0.77	19	empty

Interfaces

1 interface between chains.

A–B · 298 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

4FUP · Structural basis for Zn2+-dependent intercellular adhesion in staphylococcal biofilms · 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 Q5HKE8
Elsewhere: RCSB PDB 4FUP · PDBe 4FUP · UniProt Q5HKE8

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