MolNFT v1 · #30812 · protein
The role of histidine-40 in ribonuclease T1 catalysis: three- dimensional structures of the partially active HIS40LYS mutant
2AAE: “The role of histidine-40 in ribonuclease T1 catalysis: three- dimensional structures of the partially active…”. X-ray diffraction, 2 ligands (CA, PO4). MolNFT v1 #30812 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2AAE
- Type
- protein
- Length
- 104 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonuclease T1
- EC
- 3.1.27.3
- UniProt
- P00651
- Ligands
- CA, PO4
Structure
x-ray diffraction · 1 distinct chain · 16% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonuclease T1 (EC 3.1.27.3) | protein | 104 | 16% helix, 31% strand | P00651 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 2AAE · The role of histidine-40 in ribonuclease T1 catalysis: three-dimensional structures of… · 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 P00651
- Elsewhere: RCSB PDB 2AAE · PDBe 2AAE · UniProt P00651
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