MolNFT v1 · #23160 · protein
X-ray crystallographic and calorimeric studies of the effects of the mutation TRP 59 tyr in ribonuclease T1
1TRP · Ribonuclease T1 isozyme: “X-ray crystallographic and calorimeric studies of the effects of the mutation TRP 59 tyr in ribonuclease T1”. X-ray diffraction, 2 ligands (2GP, CA), 1 pocket (best druggability 0.28). MolNFT v1 #23160 on…
- PDB
- 1TRP
- Type
- protein
- Length
- 208 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonuclease T1 isozyme
- EC
- 3.1.27.3
- UniProt
- P00651
- Ligands
- 2GP, CA
- Pockets
- 1 · best druggability 0.28
Structure
x-ray diffraction · 1 distinct chain · 16% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Ribonuclease T1 isozyme (EC 3.1.27.3) | protein | 104 | 16% helix, 31% strand | P00651 |
Ligands and binding sites
- 2GP · Guanosine-2'-monophosphate · ligand · 2 copies · chains A, B
- CA · Calcium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 56 | 0.28 | 0.74 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 162 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1TRP · X-ray crystallographic and calorimeric studies of the effects of the mutation TRP 59 tyr… · the same entry in another collection · chain B against B, 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 P00651
- Elsewhere: RCSB PDB 1TRP · PDBe 1TRP · UniProt P00651
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