MolNFT v1 · #190731 · protein

Dimeric structure of a quorum-quenching metallo-hydrolase, lrsl

7Y7U · Mbl fold metallo-hydrolase: “Dimeric structure of a quorum-quenching metallo-hydrolase, lrsl”. X-ray diffraction, 1 ligand (ZN), 6 pockets (best druggability 0.82). MolNFT v1 #190731 on GenesisL1: 3D structure, binding sites and…

PDB: 7Y7U
Type: protein
Length: 576 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mbl fold metallo-hydrolase
UniProt: A0A222F232
Ligands: ZN
Pockets: 6 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Mbl fold metallo-hydrolase	protein	288	26% helix, 30% strand	A0A222F232

Ligands and binding sites

ZN · Zinc ion · metal · 4 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	1128	0.82	0.83	83	empty
2	310	0.58	0.77	41	empty
3	127	0.54	0.81	20	empty
4	119	0.53	0.81	18	empty
5	63	0.38	0.78	13	empty

Interfaces

1 interface between chains.

A–B · 1194 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

7Y7U · Dimeric structure of a Quorum-Quenching metallo-hydrolase, LrsL · 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 A0A222F232
Elsewhere: RCSB PDB 7Y7U · PDBe 7Y7U · UniProt A0A222F232

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