MolNFT v1 · #97111 · protein

Peptidoglycan O-acetylesterase in action, 0 min

4K40 · Gdsl-like LIPASE/ACYLHYDROLASE family protein: “Peptidoglycan O-acetylesterase in action, 0 min”. X-ray diffraction, 5 pockets (best druggability 0.74). MolNFT v1 #97111 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4K40
Type: protein
Length: 698 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Gdsl-like LIPASE/ACYLHYDROLASE family protein
UniProt: A0A0A8F713
Pockets: 5 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Gdsl-like LIPASE/ACYLHYDROLASE family protein	protein	349	31% helix, 29% strand	A0A0A8F713

Pockets

5 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	1134	0.74	0.77	94	empty
2	72	0.44	0.82	19	empty
3	55	0.36	0.80	16	empty
4	58	0.35	0.78	17	empty
5	55	0.34	0.78	16	empty

Interfaces

1 interface between chains.

A–B · 645 Å² buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

4K40 · Peptidoglycan O-acetylesterase in action, 0 min · 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 A0A0A8F713
Elsewhere: RCSB PDB 4K40 · PDBe 4K40 · UniProt A0A0A8F713

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