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Crystal structure of active HIV-1 protease in complex with the N terminal product of the substrate ma-ca.

Analyse Crystal structure of active HIV-1 protease in complex with the N terminal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4F74
Type: protein
Length: 202 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protease; N terminal product of substrate ma-ca
EC: 3.4.23.16
UniProt: P03369
Pockets: 1 · best druggability 0.59

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, 55% strand	P03369
C	N terminal product of substrate ma-ca	protein	4	0% helix, 50% strand	—

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	173	0.59	0.82	27	empty

Interfaces

3 interfaces between chains.

A–B · 1819 Å² buried · 36 hydrogen bonds · protein-protein
A–C · 329 Å² buried · 14 hydrogen bonds · protein-protein
B–C · 255 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

4F74 · Crystal Structure of active HIV-1 Protease in Complex with the N terminal product of the… · 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
Elsewhere: RCSB PDB 4F74 · PDBe 4F74 · UniProt P03369

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