MolNFT v1 · #91568 · protein

High-resolution structure of apo wt shv-1 beta-lactamase

4FH4 · Beta-lactamase shv-1: “High-resolution structure of apo wt shv-1 beta-lactamase”. X-ray diffraction, 1 ligand (MA4), 2 pockets (best druggability 0.69). MolNFT v1 #91568 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4FH4
Type: protein
Length: 265 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-lactamase shv-1
EC: 3.5.2.6
UniProt: P0AD64
Ligands: MA4
Pockets: 2 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-lactamase shv-1 (EC 3.5.2.6)	protein	265	45% helix, 17% strand	P0AD64

Ligands and binding sites

MA4 · Cyclohexyl-hexyl-beta-D-maltoside · ligand · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	201	0.69	0.86	24	empty
2	71	0.29	0.74	18	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

4FH4 · high-resolution structure of apo wt SHV-1 beta-lactamase · the same entry in another collection · chain A against A, TM-score 1.00
P0AD64 · AlphaFold monomer V2.0 prediction for beta-lactamase shv-1 (P0AD64) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P0AD64
Elsewhere: RCSB PDB 4FH4 · PDBe 4FH4 · UniProt P0AD64

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