MolNFT v1 · #37021 · protein

Crystal structure of wild-type inactive (D25N) HIV-1 protease complexed with wild-type HIV-1 nc-P1 substrate.

2FNS: “Crystal structure of wild-type inactive (D25N) HIV-1 protease complexed with wild-type HIV-1 nc-P1 substrate.”. X-ray diffraction, 1 ligand (PO4). MolNFT v1 #37021 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2FNS
Type: protein
Length: 205 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protease; Nc-P1 substrate peptide
EC: 3.4.23.16
UniProt: O38716
Ligands: PO4

Structure

x-ray diffraction · 2 distinct chains · 4% helix, 54% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Protease (EC 3.4.23.16)	protein	99	4% helix, 56% strand	O38716
P	Nc-P1 substrate peptide	protein	7	0% helix, 29% strand	—

Ligands and binding sites

PO4 · Phosphate ion · ion · chains B
ACT · Acetate ion · additive · 2 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 · 1761 Å² buried · 37 hydrogen bonds · protein-protein
A–P · 458 Å² buried · 8 hydrogen bonds · protein-protein
B–P · 366 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

2FNS · Crystal structure of wild-type inactive (D25N) HIV-1 protease complexed with wild-type… · 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 O38716
Elsewhere: RCSB PDB 2FNS · PDBe 2FNS · UniProt O38716

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