MolNFT v1 · #92486 · protein

Crystal structures of N-acyl homoserine lactonase aidh E219G mutant

4G9G · ALPHA/BETA hydrolase fold protein: “Crystal structures of N-acyl homoserine lactonase aidh E219G mutant”. X-ray diffraction, 1 ligand (NI), 5 pockets (best druggability 0.75). MolNFT v1 #92486 on GenesisL1: 3D structure, binding…

PDB: 4G9G
Type: protein
Length: 550 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ALPHA/BETA hydrolase fold protein
UniProt: D2J2T6
Ligands: NI
Pockets: 5 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ALPHA/BETA hydrolase fold protein	protein	275	45% helix, 18% strand	D2J2T6
B	ALPHA/BETA hydrolase fold protein	protein	275	45% helix, 18% strand	D2J2T6

Ligands and binding sites

NI · Nickel (II) ion · metal · 2 copies · chains A, B

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

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	141	0.75	0.93	28	NI
2	200	0.73	0.89	28	empty
3	134	0.66	0.88	37	empty
4	195	0.49	0.76	27	empty
5	180	0.49	0.76	19	empty

Interfaces

1 interface between chains.

A–B · 1002 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

4G9G · Crystal structures of N-acyl homoserine lactonase AidH E219G mutant · 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 D2J2T6
Elsewhere: RCSB PDB 4G9G · PDBe 4G9G · UniProt D2J2T6

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