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Crystal structure of AP2V substrate variant of nc-P1 decamer peptide in complex with V82A/D25N HIV-1 protease mutant

Analyse Crystal structure of AP2V substrate variant of nc-P1 decamer peptide in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1TSQ
Type: protein
Length: 208 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pol polyprotein; AP2V nc-P1 substrate peptide
EC: 3.4.23.16
UniProt: P03369, P04591

Structure

x-ray diffraction · 2 distinct chains · 4% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Pol polyprotein (EC 3.4.23.16)	protein	99	4% helix, 58% strand	P03369
P	AP2V nc-P1 substrate peptide	protein	10	0% helix, 30% strand	P04591

Ligands and binding sites

ACT · Acetate ion · additive · 10 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Interfaces

3 interfaces between chains.

A–B · 1831 Å² buried · 42 hydrogen bonds · protein-protein
B–P · 572 Å² buried · 13 hydrogen bonds · protein-protein
A–P · 509 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

1TSQ · Crystal structure of AP2V substrate variant of nc-P1 decamer peptide in complex with… · 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 P03369
Every structure of UniProt P04591
Elsewhere: RCSB PDB 1TSQ · PDBe 1TSQ · UniProt P03369 · UniProt P04591

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