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6MCR

X-ray crystal structure of wild type HIV-1 protease in complex with GRL-001

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue EDO A 101
ChainResidue
AMET46
AGLY49
AGLY52
APHE53

site_idAC2
Number of Residues3
Detailsbinding site for residue EDO A 102
ChainResidue
AGLU21
AVAL82
AASN83

site_idAC3
Number of Residues3
Detailsbinding site for residue EDO A 103
ChainResidue
ALEU19
ATRP6
AGLN18

site_idAC4
Number of Residues19
Detailsbinding site for residue JDY A 104
ChainResidue
AASP25
AASP25
AGLY27
AGLY27
AALA28
AASP29
AASP29
AASP30
AASP30
AILE47
AGLY48
AGLY48
AGLY49
AGLY49
AILE50
APRO81
AVAL82
AHOH201
AHOH201

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL
ChainResidueDetails
AALA22-LEU33

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094
ChainResidueDetails
AASP25

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
APHE99

223532

PDB entries from 2024-08-07

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