MolNFT v1 · #118724 · protein

Ctx-M-15 in complex with fpi-1602

5FAP · Beta-lactamase: “Ctx-M-15 in complex with fpi-1602”. X-ray diffraction, 1 ligand (602), 3 pockets (best druggability 0.68). MolNFT v1 #118724 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5FAP
Type: protein
Length: 516 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-lactamase
EC: 3.5.2.6
UniProt: Q9EXV5
Ligands: 602
Pockets: 3 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, A	Beta-lactamase (EC 3.5.2.6)	protein	258	45% helix, 19% strand	Q9EXV5

Ligands and binding sites

602 · [[(3~{R},6~{S})-6-[(azetidin-3-ylcarbonylamino)carbamoyl]-1-methanoyl-piperidin-3-yl]amino] hydrogen sulfate · ligand · 2 copies · chains B, 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	430	0.68	0.80	45	602
2	353	0.66	0.80	42	empty
3	95	0.36	0.75	20	602

Interfaces

1 interface between chains.

B–A · 409 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 covalent (covalent ligand).

Compared structures

5FAP · CTX-M-15 in complex with FPI-1602 · 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 Q9EXV5
Elsewhere: RCSB PDB 5FAP · PDBe 5FAP · UniProt Q9EXV5

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