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Putative sugar kinases from synechococcus elongatus PCC7942 in complex with D-ribulose

Analyse Putative sugar kinases from synechococcus elongatus PCC7942 in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5HV7
Type: protein
Length: 421 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Probable sugar kinase
UniProt: Q31KC7
Ligands: RBL
Pockets: 3 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Probable sugar kinase	protein	421	32% helix, 23% strand	Q31KC7

Ligands and binding sites

RBL · D-ribulose · ligand · 2 copies · 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	521	0.64	0.76	49	RBL
2	101	0.40	0.76	17	empty
3	76	0.35	0.76	17	empty

Compared structures

5HV7 · Putative sugar kinases from Synechococcus elongatus PCC7942 in complex with D-ribulose · the same entry in another collection · chain A against A, TM-score 1.00
Q31KC7 · AlphaFold monomer V2.0 prediction for D-ribulose kinase (Q31KC7) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q31KC7
Elsewhere: RCSB PDB 5HV7 · PDBe 5HV7 · UniProt Q31KC7

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