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Outer membrane phospholipase a from escherichia COLI

Analyse Outer membrane phospholipase a from escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1FW3
Type: protein
Length: 500 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Outer membrane phospholipase a
EC: 3.1.1.32
UniProt: P0A921
Pockets: 9 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 7% helix, 58% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Outer membrane phospholipase a (EC 3.1.1.32)	protein	250	7% helix, 58% strand	P0A921

Pockets

9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	151	0.81	0.97	34	empty
2	156	0.80	0.96	34	empty
3	183	0.70	0.88	32	empty
4	261	0.60	0.79	33	empty
5	264	0.60	0.79	37	empty

Interfaces

1 interface between chains.

A–B · 1860 Å² buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (nonstandard).

Compared structures

1FW3 · 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 1FW3 · PDBe 1FW3 · UniProt P0A921

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