Research workbench
Structure of thermotoga maritima amidohydrolase TM0936 bound to ni and methionine
Analyse Structure of thermotoga maritima amidohydrolase TM0936 bound to ni and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1P1M
- Type
- protein
- Length
- 404 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein TM0936
- UniProt
- Q9X034
- Ligands
- MET, NI
- Pockets
- 1 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical protein TM0936 | protein | 404 | 37% helix, 24% strand | Q9X034 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 211 | 0.67 | 0.85 | 28 | MET |
Compared structures
- 1P1M · Structure of Thermotoga maritima amidohydrolase TM0936 bound to Ni and methionine · the same entry in another collection · chain A against A, TM-score 1.00
- Q9X034 · AlphaFold monomer V2.0 prediction for 5-METHYLTHIOADENOSINE/S-adenosylhomocysteine… · 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 Q9X034
- Elsewhere: RCSB PDB 1P1M · PDBe 1P1M · UniProt Q9X034
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