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X-ray crystal structure of the mouse cmp-sialic acid transporter in complex with cmp, by lipidic cubic phase

Analyse X-ray crystal structure of the mouse cmp-sialic acid transporter in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6OH2
Type: protein
Length: 299 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cmp-sialic acid transporter
UniProt: Q61420
Ligands: C5P
Pockets: 3 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 81% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cmp-sialic acid transporter	protein	299	81% helix, 0% strand	Q61420

Ligands and binding sites

C5P · Cytidine-5'-monophosphate · ligand · chains 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	477	0.85	0.92	60	C5P
2	139	0.44	0.76	23	empty
3	90	0.33	0.74	17	empty

Compared structures

6OH2 · X-ray crystal structure of the mouse CMP-sialic acid transporter in complex with CMP, by… · the same entry in another collection · chain A against A, TM-score 1.00
Q61420 · AlphaFold monomer V2.0 prediction for cmp-sialic acid transporter (Q61420) · 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 Q61420
Elsewhere: RCSB PDB 6OH2 · PDBe 6OH2 · UniProt Q61420

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