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Crystal structure of the single-chain fv fragment 1696 in complex with the epitope peptide corresponding to N- terminus of HIV-2 protease

Analyse Crystal structure of the single-chain fv fragment 1696 in complex with the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1SVZ
Type
protein
Length
476 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Single-chain fv fragment 1696; Epitope peptide corresponding to N-terminus of HIV-2…
UniProt
P01631
Pockets
4 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 8% helix, 50% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BSingle-chain fv fragment 1696protein2328% helix, 52% strandP01631
C, DEpitope peptide corresponding to N-terminus of HIV-2 proteaseprotein60% helix, 0% strand—

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110090.810.83104empty
22050.580.8034empty
3500.280.7515empty
4570.260.7315empty

Interfaces

3 interfaces between chains.

  • A–B · 840 Ų buried · 6 hydrogen bonds · protein-protein
  • B–D · 584 Ų buried · 13 hydrogen bonds · protein-protein
  • A–C · 581 Ų buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 1SVZ · Crystal structure of the single-chain Fv fragment 1696 in complex with the epitope… · the same entry in another collection · chain A against A, TM-score 1.00
  • P01631 · AlphaFold monomer V2.0 prediction for ig kappa chain V-II region 26-10 (P01631) · a predicted model of the same protein · chain A against A, TM-score 0.48

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