MolNFT v2 · #116977 · protein

Crystal structure of Acinetobacter baumannii OccAB1

5DL5 · Membrane protein: “Crystal structure of Acinetobacter baumannii OccAB1”. X-ray diffraction at 2.05, 1 ligand (PO4), 2 pockets (best druggability 0.70). MolNFT v2 #116977 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5DL5
Type: protein
Length: 416 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.05
Source: Acinetobacter baumannii AB307-0294
Molecule: Membrane protein
UniProt: A0A0F5EN03
Ligands: PO4
Pockets: 2 · best druggability 0.70

Structure

x-ray diffraction · resolution 2.05 · 1 distinct chain · 1% helix, 57% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Membrane protein	protein	416	1% helix, 57% strand	A0A0F5EN03

Ligands and binding sites

PO4 · Phosphate ion · ion · chains A
C8E · (hydroxyethyloxy)tri(ethyloxy)octane · additive · 3 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	882	0.70	0.75	91	C8E
2	64	0.29	0.73	15	empty

Compared structures

5DL5 · Crystal structure of acinetobacter baumannii OCCAB1 · 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 A0A0F5EN03
Elsewhere: RCSB PDB 5DL5 · PDBe 5DL5 · UniProt A0A0F5EN03

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