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1GNO

HIV-1 PROTEASE (WILD TYPE) COMPLEXED WITH U89360E (INHIBITOR)

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 Residues24
DetailsBINDING SITE FOR RESIDUE U0E B 100
ChainResidue
AARG8
BGLY27
BALA28
BASP29
BASP30
BILE47
BGLY48
BGLY49
BILE50
BPRO81
BVAL82
ALEU23
BU0E101
BU0E101
BHOH112
BHOH117
BHOH130
AASP25
AGLY27
AALA28
AGLY49
BARG8
BARG8
BASP25

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE U0E B 101
ChainResidue
AASP25
AGLY27
AALA28
AASP29
AASP30
AILE47
AGLY48
AGLY49
APRO81
AVAL82
BASP25
BGLY27
BGLY48
BGLY49
BU0E100
BU0E100
BHOH117
BHOH124
BHOH130

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 Residues2
DetailsACT_SITE: For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094, ECO:0000269|PubMed:12924029
ChainResidueDetails
AASP25
BASP25

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
AILE64
BILE64

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000269|PubMed:2476069
ChainResidueDetails
BPHE99
APHE99

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by host => ECO:0000250
ChainResidueDetails
AILE64
BILE64

218500

数据于2024-04-17公开中

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