Research workbench

Fic protein from neisseria meningitidis in complex with amppnp

Analyse Fic protein from neisseria meningitidis in complex with amppnp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3S6A
Type: protein
Length: 178 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell filamentation protein fic-related protein
UniProt: Q7DDR9
Ligands: ANP
Pockets: 2 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 61% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cell filamentation protein fic-related protein	protein	178	61% helix, 4% strand	Q7DDR9

Ligands and binding sites

ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	111	0.70	0.91	27	empty
2	163	0.57	0.81	26	ANP

Compared structures

3S6A · Fic protein from NEISSERIA MENINGITIDIS in complex with AMPPNP · the same entry in another collection · chain A against A, TM-score 1.00
Q7DDR9 · AlphaFold monomer V2.0 prediction for protein adenylyltransferase nmfic (Q7DDR9) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q7DDR9
Elsewhere: RCSB PDB 3S6A · PDBe 3S6A · UniProt Q7DDR9

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