MolNFT v2 · #7081 · protein

Outer membrane phospholipase a from escherichia COLI

1FW2: “Outer membrane phospholipase a from escherichia COLI”. X-ray diffraction at 2.6, 1 ligand (CA), 2 pockets (best druggability 0.78). MolNFT v2 #7081 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1FW2
Type: protein
Length: 257 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.6
Source: Escherichia coli
Molecule: Outer membrane phospholipase a
EC: 3.1.1.32
UniProt: P0A921
Ligands: CA
Pockets: 2 · best druggability 0.78

Structure

x-ray diffraction · resolution 2.6 · 1 distinct chain · 7% helix, 54% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Outer membrane phospholipase a (EC 3.1.1.32)	protein	257	7% helix, 54% strand	P0A921

Ligands and binding sites

CA · Calcium ion · metal · 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	99	0.78	0.98	30	empty
2	167	0.48	0.77	30	empty

Compared structures

1FW2 · Outer membrane phospholipase a from escherichia COLI · the same entry in another collection · chain A against A, TM-score 1.00
P0A921 · AlphaFold monomer V2.0 prediction for phospholipase A1 (P0A921) · a predicted model of the same protein · 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 P0A921
Elsewhere: RCSB PDB 1FW2 · PDBe 1FW2 · UniProt P0A921

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