MolNFT v1 · #181215 · protein

Nora in complex with FAB25

7LO7 · Quinolone resistance protein nora: “Nora in complex with FAB25”. Electron microscopy, 13 pockets (best druggability 0.83). MolNFT v1 #181215 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7LO7
Type: protein
Length: 805 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Quinolone resistance protein nora; FAB25 heavy chain; FAB25 light chain
UniProt: Q53459
Pockets: 13 · best druggability 0.83

Structure

electron microscopy · 3 distinct chains · 38% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
Z	Quinolone resistance protein nora	protein	360	78% helix, 0% strand	Q53459
H	FAB25 heavy chain	protein	232	5% helix, 35% strand	—
L	FAB25 light chain	protein	213	4% helix, 42% strand	—

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1085	0.83	0.84	99	empty
2	75	0.65	0.92	20	empty
3	77	0.56	0.87	16	empty
4	304	0.51	0.73	48	empty
5	105	0.50	0.82	18	empty

Interfaces

3 interfaces between chains.

H–L · 1956 Å² buried · 12 hydrogen bonds · protein-protein
Z–H · 1300 Å² buried · 9 hydrogen bonds · protein-protein
Z–L · 202 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

7LO7 · NorA in complex with Fab25 · the same entry in another collection · chain Z against Z, 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 Q53459
Elsewhere: RCSB PDB 7LO7 · PDBe 7LO7 · UniProt Q53459

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