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Crystal structure of cdp-chase

Analyse Crystal structure of cdp-chase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3Q1P
Type: protein
Length: 398 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphohydrolase (MUTT/NUDIX family protein)
UniProt: Q81EE8
Ligands: SO4
Pockets: 6 · best druggability 0.67

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphohydrolase (MUTT/NUDIX family protein)	protein	201	38% helix, 27% strand	Q81EE8
B	Phosphohydrolase (MUTT/NUDIX family protein)	protein	197	32% helix, 28% strand	Q81EE8

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A, B

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

Pockets

6 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	542	0.67	0.77	44	empty
2	250	0.54	0.77	35	empty
3	65	0.53	0.87	25	empty
4	79	0.38	0.77	13	empty
5	79	0.33	0.74	19	empty

Interfaces

1 interface between chains.

A–B · 3297 Å² buried · 30 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

3Q1P · Crystal structure of CDP-Chase · 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 Q81EE8
Elsewhere: RCSB PDB 3Q1P · PDBe 3Q1P · UniProt Q81EE8

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