Research workbench
Structure of chaetomium thermophilum MAPE1
Analyse Structure of chaetomium thermophilum MAPE1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5JM6
- Type
- protein
- Length
- 2,670 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aminopeptidase-like protein
- UniProt
- G0SG74
- Ligands
- ZN
- Pockets
- 20 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E, F, B, C, D | Aminopeptidase-like protein | protein | 445 | 29% helix, 24% strand | G0SG74 |
Ligands and binding sites
- ZN · Zinc ion · metal · 12 copies · chains A, E, F, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 931 | 0.86 | 0.87 | 75 | empty |
| 2 | 1066 | 0.84 | 0.85 | 77 | empty |
| 3 | 944 | 0.76 | 0.79 | 101 | empty |
| 4 | 921 | 0.76 | 0.79 | 105 | ZN |
| 5 | 635 | 0.74 | 0.81 | 101 | empty |
Interfaces
7 interfaces between chains.
- E–C · 3559 Ų buried · 58 hydrogen bonds · protein-protein
- A–B · 1488 Ų buried · 21 hydrogen bonds · protein-protein
- A–C · 1453 Ų buried · 27 hydrogen bonds · protein-protein
- B–C · 1445 Ų buried · 20 hydrogen bonds · protein-protein
- E–D · 1425 Ų buried · 20 hydrogen bonds · protein-protein
Compared structures
- 5JM6 · Structure of Chaetomium thermophilum mApe1 · 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 G0SG74
- Elsewhere: RCSB PDB 5JM6 · PDBe 5JM6 · UniProt G0SG74
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