Research workbench
Calcium binding to thermitase. crystallographic studies of thermitase at 0, 5 and 100 mm calcium
Analyse Calcium binding to thermitase. crystallographic studies of thermitase at 0, 5… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TEC
- Type
- protein
- Length
- 342 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thermitase; Eglin C
- EC
- 3.4.21.66
- UniProt
- P04072, P01051
- Ligands
- CA
- Pockets
- 1 · best druggability 0.60
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | Thermitase (EC 3.4.21.66) | protein | 279 | 29% helix, 22% strand | P04072 |
| I | Eglin C | protein | 63 | 22% helix, 35% strand | P01051 |
Ligands and binding sites
- CA · Calcium ion · metal · 3 copies · chains E
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 | 234 | 0.60 | 0.80 | 29 | empty |
Interfaces
1 interface between chains.
- E–I · 779 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 3TEC · Calcium binding to thermitase. crystallographic studies of thermitase at 0, 5 and 100 mm… · the same entry in another collection · chain E against E, TM-score 1.00
- P04072 · AlphaFold monomer V2.0 prediction for thermitase (P04072) · a predicted model of the same protein · chain E against A, TM-score 1.00
- P01051 · AlphaFold monomer V2.0 prediction for eglin C (P01051) · a predicted model of the same protein · chain I 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 P04072
- Every structure of UniProt P01051
- Elsewhere: RCSB PDB 3TEC · PDBe 3TEC · UniProt P04072 · UniProt P01051
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