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2HB3

Wild-type HIV-1 Protease in complex with potent inhibitor GRL06579

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
A0042802molecular_functionidentical protein binding
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
B0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 901
ChainResidue
ATHR74
AASN88
BARG41

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 902
ChainResidue
BTRP6

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 903
ChainResidue
BTHR74
BASN88
BHOH1020

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 904
ChainResidue
AHOH1045
AHOH1064
AHOH1098
AHOH1144
AASP60
AHOH1041

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA B 905
ChainResidue
BASP60
BHOH1044
BHOH1066
BHOH1103
BHOH1115

site_idAC6
Number of Residues20
DetailsBINDING SITE FOR RESIDUE GRL B 201
ChainResidue
AARG8
AASP25
AGLY27
AALA28
AASP29
AASP30
AVAL32
AGLY48
AGLY49
AVAL82
AILE84
AHOH1191
BASP25
BGLY27
BALA28
BASP29
BGLY48
BGLY49
BILE50
BHOH1009

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 906
ChainResidue
AGLY94
BTRP42
BARG57
BHOH1080

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVI
ChainResidueDetails
AALA22-ILE33

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, ECO:0000269|PubMed:12924029
ChainResidueDetails
BTHR26
ATHR26

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease
ChainResidueDetails
BPRO1
APRO1

221051

PDB entries from 2024-06-12

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