MolNFT v1 · #118424 · protein

Crystal structure of ampc ber adenylylated in the cytoplasm

5F1G · Beta-lactamase: “Crystal structure of ampc ber adenylylated in the cytoplasm”. X-ray diffraction, 2 ligands (AMP, SO4), 3 pockets (best druggability 0.55). MolNFT v1 #118424 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 5F1G
Type: protein
Length: 351 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-lactamase
EC: 3.5.2.6
UniProt: A7TUE6
Ligands: AMP, SO4
Pockets: 3 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-lactamase (EC 3.5.2.6)	protein	351	39% helix, 23% strand	A7TUE6

Ligands and binding sites

AMP · Adenosine monophosphate · ligand · chains A
SO4 · Sulfate ion · ion · chains A
EDO · 1,2-ethanediol · additive · 2 copies · chains A

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

Pockets

3 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	313	0.55	0.76	54	AMP, SO4
2	122	0.38	0.73	28	EDO
3	61	0.27	0.73	11	empty

Modifications

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

Compared structures

5F1G · Crystal structure of AmpC BER adenylylated in the cytoplasm · 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 A7TUE6
Elsewhere: RCSB PDB 5F1G · PDBe 5F1G · UniProt A7TUE6

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