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Crystal structure of cmp bound cst in an outward facing conformation

Analyse Crystal structure of cmp bound cst in an outward facing conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6I1R
Type: protein
Length: 619 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cmp-sialic acid transporter 1
UniProt: B4FZ94
Ligands: C5P
Pockets: 9 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 73% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cmp-sialic acid transporter 1	protein	309	73% helix, 0% strand	B4FZ94
B	Cmp-sialic acid transporter 1	protein	310	73% helix, 0% strand	B4FZ94

Ligands and binding sites

C5P · Cytidine-5'-monophosphate · ligand · 2 copies · chains A, B

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

Pockets

9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	801	0.79	0.82	58	C5P
2	931	0.79	0.81	59	C5P
3	199	0.56	0.79	42	empty
4	183	0.49	0.77	25	empty
5	188	0.48	0.76	26	empty

Interfaces

1 interface between chains.

A–B · 950 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

6I1R · Crystal structure of CMP bound CST in an outward facing conformation · 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 B4FZ94
Elsewhere: RCSB PDB 6I1R · PDBe 6I1R · UniProt B4FZ94

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