MolNFT v1 · #125844 · protein

Crystal structure of kpc-2 carbapenemase in complex with a phenyl boronic inhibitor.

5LL7 · Beta-lactamase: “Crystal structure of kpc-2 carbapenemase in complex with a phenyl boronic inhibitor.”. X-ray diffraction, 1 ligand (6YV), 1 pocket (best druggability 0.28). MolNFT v1 #125844 on GenesisL1: 3D structure, binding…

PDB: 5LL7
Type: protein
Length: 264 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-lactamase
EC: 3.5.2.6
UniProt: A0A0H4IUK8
Ligands: 6YV
Pockets: 1 · best druggability 0.28

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-lactamase (EC 3.5.2.6)	protein	264	43% helix, 17% strand	A0A0H4IUK8

Ligands and binding sites

6YV · (~{E})-3-[2-(dihydroxyboranyl)phenyl]prop-2-enoic acid · ligand · chains A
EDO · 1,2-ethanediol · additive · 3 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	71	0.28	0.73	18	6YV

Modifications

Observed in the structure: 1 covalent, 1 disulfide (covalent ligand, disulfide).

Compared structures

5LL7 · Crystal structure of KPC-2 carbapenemase in complex with a phenyl boronic inhibitor. · 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 A0A0H4IUK8
Elsewhere: RCSB PDB 5LL7 · PDBe 5LL7 · UniProt A0A0H4IUK8

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