MolNFT v1 · #115194 · protein

Joint X-RAY/NEUTRON structure of mtan D198N complex with sah

5CCD · Aminodeoxyfutalosine nucleosidase: “Joint X-RAY/NEUTRON structure of mtan D198N complex with sah”. X-ray diffraction; neutron diffraction, 1 ligand (SAH), 1 pocket (best druggability 0.61). MolNFT v1 #115194 on GenesisL1: 3D…

PDB: 5CCD
Type: protein
Length: 230 residues
Chains: 1
Method: x-ray diffraction; neutron diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aminodeoxyfutalosine nucleosidase
EC: 3.2.2.30, 3.2.2.9
UniProt: Q9ZMY2
Ligands: SAH
Pockets: 1 · best druggability 0.61

Structure

x-ray diffraction; neutron diffraction · 1 distinct chain · 38% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aminodeoxyfutalosine nucleosidase (EC 3.2.2.30, 3.2.2.9)	protein	230	38% helix, 28% strand	Q9ZMY2

Ligands and binding sites

SAH · S-adenosyl-L-homocysteine · ligand · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	77	0.61	0.90	19	SAH

Compared structures

5CCD · Joint X-ray/neutron structure of MTAN D198N complex with SAH · the same entry in another collection · chain A against A, TM-score 1.00
Q9ZMY2 · AlphaFold monomer V2.0 prediction for aminodeoxyfutalosine nucleosidase (Q9ZMY2) · a predicted model of the same protein · 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 Q9ZMY2
Elsewhere: RCSB PDB 5CCD · PDBe 5CCD · UniProt Q9ZMY2

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