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Cyanovirin-N double mutant P51S S52P

Analyse Cyanovirin-N double mutant P51S S52P in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1LOM
Type: protein
Length: 101 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cyanovirin-N
UniProt: P81180
Ligands: CA, SO4

Structure

x-ray diffraction · 1 distinct chain · 10% helix, 57% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cyanovirin-N	protein	101	10% helix, 57% strand	P81180

Ligands and binding sites

CA · Calcium ion · metal · 2 copies · chains A
SO4 · Sulfate ion · ion · chains A

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

1LOM · Cyanovirin-N double mutant P51S S52P · the same entry in another collection · chain A against A, TM-score 1.00
P81180 · AlphaFold monomer V2.0 prediction for cyanovirin-N (P81180) · a predicted model of the same protein · chain A against A, TM-score 0.49

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 P81180
Elsewhere: RCSB PDB 1LOM · PDBe 1LOM · UniProt P81180

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