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Crystal structure of cmp kinase from thermus thermophilus HB8

Analyse Crystal structure of cmp kinase from thermus thermophilus HB8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3W90
Type: protein
Length: 198 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytidylate kinase
EC: 2.7.4.25
UniProt: Q5SL35
Pockets: 2 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytidylate kinase (EC 2.7.4.25)	protein	198	52% helix, 16% strand	Q5SL35

Pockets

2 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	263	0.54	0.76	28	empty
2	63	0.34	0.77	15	empty

Compared structures

3W90 · Crystal structure of CMP kinase from Thermus thermophilus HB8 · the same entry in another collection · chain A against A, TM-score 1.00
Q5SL35 · AlphaFold monomer V2.0 prediction for cytidylate kinase (Q5SL35) · a predicted model of the same protein · chain A against A, TM-score 0.76

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 Q5SL35
Elsewhere: RCSB PDB 3W90 · PDBe 3W90 · UniProt Q5SL35

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