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Crystal structure analysis of the monomeric [S- carboxyamidomethyl-CYS31, S-carboxyamidomethyl-CYS32] bovine seminal ribonuclease

Analyse Crystal structure analysis of the monomeric [S- carboxyamidomethyl-CYS31… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1N1X
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

Structure

x-ray diffraction · 1 distinct chain · 22% helix, 37% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARibonuclease, seminal (EC 3.1.27.5)protein11922% helix, 37% strandP00669

Modifications

Observed in the structure: 4 disulfide, 2 modified (disulfide, alkylation).

Compared structures

  • 1N1X · Crystal Structure Analysis of the monomeric [S-carboxyamidomethyl-Cys31… · 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

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