MolNFT v1 · #19491 · protein

The atomic resolution structure of a novel bacterial esterase

1QLW: “The atomic resolution structure of a novel bacterial esterase”. X-ray diffraction, 1 ligand (SO4), 6 pockets (best druggability 0.78). MolNFT v1 #19491 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1QLW
Type: protein
Length: 635 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Esterase
Ligands: SO4
Pockets: 6 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Esterase	protein	318	34% helix, 20% strand	—
B	Esterase	protein	317	34% helix, 21% strand	—

Ligands and binding sites

SO4 · Sulfate ion · ion · 3 copies · chains A, B

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

Pockets

6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	92	0.78	0.98	20	empty
2	63	0.69	0.97	25	empty
3	209	0.54	0.78	32	SO4
4	152	0.53	0.80	34	empty
5	72	0.40	0.79	17	empty

Interfaces

1 interface between chains.

A–B · 2945 Å² buried · 53 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

1QLW · The Atomic Resolution Structure of a Novel Bacterial Esterase · 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
Elsewhere: RCSB PDB 1QLW · PDBe 1QLW

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