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Imp-6 metallo-beta-lactamase

Analyse Imp-6 metallo-beta-lactamase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6LVJ
Type: protein
Length: 854 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-lactamase
EC: 3.5.2.6
UniProt: K4PWX3
Ligands: ZN
Pockets: 9 · best druggability 0.75

Structure

x-ray diffraction · 3 distinct chains · 27% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Beta-lactamase (EC 3.5.2.6)	protein	216	26% helix, 32% strand	K4PWX3
C	Beta-lactamase (EC 3.5.2.6)	protein	210	28% helix, 30% strand	K4PWX3
D	Beta-lactamase (EC 3.5.2.6)	protein	212	28% helix, 30% strand	K4PWX3

Ligands and binding sites

ZN · Zinc ion · metal · 8 copies · chains A, B, C, D

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

Pockets

9 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	434	0.75	0.84	48	empty
2	440	0.73	0.83	49	empty
3	391	0.62	0.77	44	empty
4	240	0.50	0.75	38	empty
5	177	0.50	0.77	27	empty

Interfaces

3 interfaces between chains.

A–D · 707 Å² buried · 4 hydrogen bonds · protein-protein
B–C · 639 Å² buried · 3 hydrogen bonds · protein-protein
A–B · 456 Å² buried · 10 hydrogen bonds · protein-protein

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 K4PWX3
Elsewhere: RCSB PDB 6LVJ · PDBe 6LVJ · UniProt K4PWX3

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