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X-ray crystal structure of ampc beta-lactamase (AMPC(D)) from an escherichia COLI with a tripeptide deletion (GLY286 SER287 ASP288) on the H10 helix

Analyse X-ray crystal structure of ampc beta-lactamase (AMPC(D)) from an escherichia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2ZJ9
Type: protein
Length: 710 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ampc
EC: 3.5.2.6
UniProt: Q5EET9
Ligands: NA
Pockets: 5 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Ampc (EC 3.5.2.6)	protein	355	41% helix, 23% strand	Q5EET9

Ligands and binding sites

NA · Sodium ion · metal · 2 copies · chains A, B
IPA · Isopropyl alcohol · additive · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	229	0.52	0.76	39	empty
2	246	0.51	0.75	40	empty
3	99	0.34	0.73	24	empty
4	71	0.33	0.75	16	empty
5	78	0.31	0.73	19	empty

Compared structures

2ZJ9 · X-ray crystal structure of AmpC beta-Lactamase (AmpC(D)) from an Escherichia coli with a… · 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 Q5EET9
Elsewhere: RCSB PDB 2ZJ9 · PDBe 2ZJ9 · UniProt Q5EET9

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