Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7M9T

HIV-1 Protease WT (NL4-3) in Complex with NR02-73

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue SO4 B 101
ChainResidue
BLYS20
BGLU21
BASN83
BHOH234

site_idAC2
Number of Residues19
Detailsbinding site for residue YUD A 101
ChainResidue
AGLY48
AGLY49
AILE50
AHOH214
BASP25
BGLY27
BALA28
BASP29
BASP30
BVAL32
BGLY48
BGLY49
BILE84
BHOH201
AASP25
AGLY27
AALA28
AASP29
AASP30

site_idAC3
Number of Residues4
Detailsbinding site for residue SO4 A 102
ChainResidue
ALYS7
AARG8
ALEU10
AHOH210

site_idAC4
Number of Residues5
Detailsbinding site for residue SO4 A 103
ChainResidue
AASN37
AHOH201
AHOH202
BPRO39
BGLY40

site_idAC5
Number of Residues5
Detailsbinding site for residue SO4 A 104
ChainResidue
AGLY68
AHIS69
ALYS70
AHOH203
BPRO1

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL
ChainResidueDetails
BALA22-LEU33

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094
ChainResidueDetails
BASP25
AASP25

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
BPHE99
APHE99

225946

PDB entries from 2024-10-09

PDB statisticsPDBj update infoContact PDBjnumon