Research workbench
Mutant monomer of recombinant human hexokinase type I complexed with glucose, glucose-6-phosphate, and ADP
Analyse Mutant monomer of recombinant human hexokinase type I complexed with glucose… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CZA
- Type
- protein
- Length
- 898 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hexokinase type I
- EC
- 2.7.1.1
- UniProt
- P19367
- Ligands
- ADP, GLC, G6P
- Pockets
- 7 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| N | Hexokinase type I (EC 2.7.1.1) | protein | 898 | 45% helix, 19% strand | P19367 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains N
- GLC · alpha-D-glucopyranose · sugar · 2 copies · chains N
- G6P · 6-O-phosphono-alpha-D-glucopyranose · sugar · 2 copies · chains N
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 189 | 0.67 | 0.86 | 37 | GLC, G6P |
| 2 | 138 | 0.58 | 0.84 | 23 | G6P |
| 3 | 324 | 0.54 | 0.75 | 35 | empty |
| 4 | 262 | 0.54 | 0.77 | 42 | empty |
| 5 | 230 | 0.52 | 0.76 | 38 | empty |
Compared structures
- 1CZA · Mutant monomer of recombinant human hexokinase type I complexed with glucose… · the same entry in another collection · chain N against N, TM-score 1.00
- P19367 · AlphaFold monomer V2.0 prediction for hexokinase-1 (P19367) · a predicted model of the same protein · chain N against A, TM-score 0.95
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 P19367
- Elsewhere: RCSB PDB 1CZA · PDBe 1CZA · UniProt P19367
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