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6O48

Wild-type HIV-1 protease in complex with a substrate analog CA-p2

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 NA A 501
ChainResidue
AASP60
AHOH619
AHOH621
AHOH626
AHOH630
AHOH639

site_idAC2
Number of Residues4
Detailsbinding site for residue CL A 502
ChainResidue
BARG41
AGLY73
ATHR74
AASN88

site_idAC3
Number of Residues6
Detailsbinding site for residue FMT A 503
ChainResidue
AARG87
AASN88
ATHR91
AHOH629
BLEU5
BARG41

site_idAC4
Number of Residues27
Detailsbinding site for residue 0Q4 B 201
ChainResidue
ATRP6
AARG8
ALEU23
AASP25
AGLY27
AALA28
AASP29
AGLY48
AGLY49
APRO81
AVAL82
BASP25
BGLY27
BALA28
BASP29
BASP30
BLYS45
BMET46
BILE47
BGLY48
BGLY49
BILE50
BVAL82
BILE84
BHOH303
BHOH314
BHOH336

site_idAC5
Number of Residues1
Detailsbinding site for residue CL B 202
ChainResidue
BTRP6

site_idAC6
Number of Residues9
Detailsbinding site for residue GOL B 203
ChainResidue
AGLN18
AMET36
ASER37
BTHR12
BGLU65
BILE66
BALA67
BGLY68
BHOH318

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
AASP25
BASP25

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000269|PubMed:2476069
ChainResidueDetails
APHE99
BPHE99

218853

数据于2024-04-24公开中

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