Research workbench
Divalent metal cofactor binding in the kinetic folding trajectory of E. COLI ribonuclease hi
Analyse Divalent metal cofactor binding in the kinetic folding trajectory of E. COLI… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1F21
- Type
- protein
- Length
- 152 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonuclease hi
- EC
- 3.1.26.4
- UniProt
- P0A7Y4
- Pockets
- 2 · best druggability 0.30
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonuclease hi (EC 3.1.26.4) | protein | 152 | 37% helix, 31% strand | P0A7Y4 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 56 | 0.30 | 0.75 | 15 | empty |
| 2 | 54 | 0.28 | 0.74 | 14 | empty |
Compared structures
- 1F21 · Divalent metal cofactor binding in the kinetic folding trajectory of E. COLI ribonuclease… · the same entry in another collection · chain A against A, TM-score 1.00
- P0A7Y4 · AlphaFold monomer V2.0 prediction for ribonuclease hi (P0A7Y4) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P0A7Y4
- Elsewhere: RCSB PDB 1F21 · PDBe 1F21 · UniProt P0A7Y4
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