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Structure of mycobacterium thermoresistibile glge in complex with maltose (cocrystallisation with maltose-1-phosphate) at 3.32A resolution
Analyse Structure of mycobacterium thermoresistibile glge in complex with maltose… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CIM
- Type
- protein
- Length
- 1,311 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-1,4-GLUCAN:MALTOSE-1-phosphate maltosyltransferase
- EC
- 2.4.99.16
- UniProt
- G7CL00
- Ligands
- GLC
- Pockets
- 14 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-1,4-GLUCAN:MALTOSE-1-phosphate maltosyltransferase (EC 2.4.99.16) | protein | 636 | 35% helix, 26% strand | G7CL00 |
| B | Alpha-1,4-GLUCAN:MALTOSE-1-phosphate maltosyltransferase (EC 2.4.99.16) | protein | 675 | 31% helix, 25% strand | G7CL00 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1090 | 0.75 | 0.78 | 70 | GLC |
| 2 | 312 | 0.69 | 0.83 | 46 | empty |
| 3 | 601 | 0.63 | 0.74 | 74 | empty |
| 4 | 118 | 0.51 | 0.81 | 22 | empty |
| 5 | 119 | 0.47 | 0.79 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1776 Ų buried · 36 hydrogen bonds · protein-protein
Compared structures
- 5CIM · Structure of Mycobacterium thermoresistibile GlgE in complex with maltose… · 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 G7CL00
- Elsewhere: RCSB PDB 5CIM · PDBe 5CIM · UniProt G7CL00
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