Research workbench
Crystal structure of the [S-carboxyamidomethyl-CYS31, S- carboxyamidomethyl-CYS32] monomeric derivative of the bovine seminal ribonuclease in the liganded state
Analyse Crystal structure of the [S-carboxyamidomethyl-CYS31, S… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1N3Z
- Type
- protein
- Length
- 119 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonuclease, seminal
- EC
- 3.1.27.5
- UniProt
- P00669
- Ligands
- U3P, ADN
Structure
x-ray diffraction · 1 distinct chain · 22% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonuclease, seminal (EC 3.1.27.5) | protein | 119 | 22% helix, 37% strand | P00669 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 4 disulfide, 2 modified (disulfide, alkylation).
Compared structures
- 1N3Z · Crystal structure of the [S-carboxyamidomethyl-Cys31, S-carboxyamidomethyl-Cys32]… · the same entry in another collection · chain A against A, TM-score 1.00
- P00669 · AlphaFold monomer V2.0 prediction for seminal ribonuclease (P00669) · 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 P00669
- Elsewhere: RCSB PDB 1N3Z · PDBe 1N3Z · UniProt P00669
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