MolNFT v1 · #10269 · protein

Outer membrane phospholipase a from escherichia COLI N156A active site mutant pH 8.3

1IM0 · Outer membrane phsopholipase a: “Outer membrane phospholipase a from escherichia COLI N156A active site mutant pH 8.3”. X-ray diffraction, 1 pocket (best druggability 0.69). MolNFT v1 #10269 on GenesisL1: 3D structure, binding sites…

PDB: 1IM0
Type: protein
Length: 262 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Outer membrane phsopholipase a
EC: 3.1.1.32
UniProt: P0A921
Pockets: 1 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 8% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Outer membrane phsopholipase a (EC 3.1.1.32)	protein	262	8% helix, 55% strand	P0A921

Ligands and binding sites

BOG · octyl beta-D-glucopyranoside · additive · 4 copies · chains A
MPD · (4S)-2-methyl-2,4-pentanediol · additive · 3 copies · chains A

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	282	0.69	0.84	58	MPD

Compared structures

1IM0 · Outer membrane phospholipase a from escherichia COLI N156A active site mutant pH 8.3 · 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 0.99

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 1IM0 · PDBe 1IM0 · UniProt P0A921

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