MolNFT v1 · #12520 · protein

Substrate shape determines specificity of recognition recognition for HIV-1 protease: analysis of crystal structures of six substrate complexes

1KJF · Pol polyprotein: “Substrate shape determines specificity of recognition recognition for HIV-1 protease: analysis of crystal…”. X-ray diffraction. MolNFT v1 #12520 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1KJF
Type: protein
Length: 208 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pol polyprotein; Gag polyprotein
EC: 3.4.23.16
UniProt: P03369, P20875

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 56% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Pol polyprotein (EC 3.4.23.16)	protein	99	7% helix, 58% strand	P03369
P	Gag polyprotein	protein	10	0% helix, 40% strand	P20875

Ligands and binding sites

ACT · Acetate ion · additive · 4 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 · 1855 Å² buried · 36 hydrogen bonds · protein-protein
B–P · 604 Å² buried · 14 hydrogen bonds · protein-protein
A–P · 477 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

1KJF · Substrate shape determines specificity of recognition recognition for HIV-1 protease… · 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 P20875
Elsewhere: RCSB PDB 1KJF · PDBe 1KJF · UniProt P03369 · UniProt P20875

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