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3BXS

Crystal Structures Of Highly Constrained Substrate And Hydrolysis Products Bound To HIV-1 Protease. Implications For Catalytic Mechanism

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 Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 601
ChainResidue
AHIS69
ALYS70
AHOH375
AHOH501
BPRO101
BLYS155

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 602
ChainResidue
AHOH349
BHOH425
APRO1
AARG57
AHIS69

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 603
ChainResidue
AARG14
AGLY17
AHOH334
AHOH443
BARG114
BILE115
BGLY116
BGLY117
BHOH357
BHOH432

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE DRS A 201
ChainResidue
AASP25
AGLY27
AALA28
AASP29
AGLY48
AGLY49
AHOH468
BARG108
BLEU123
BASP125
BILE150
BPRO181
BHOH301

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE DRS B 203
ChainResidue
AARG8
AASP25
APRO81
AILE84
BGLY127
BALA128
BASP129
BASP130
BILE147
BGLY148
BGLY149
BHOH301
BHOH452

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
ChainResidueDetails
AASP25
BASP125

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
APHE99
BPHE199

218853

数据于2024-04-24公开中

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