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7MA5

HIV-1 Protease (I84V) in Complex with UMass4

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 Residues8
Detailsbinding site for residue SO4 B 101
ChainResidue
ALYS14
BLYS14
BILE15
BGLY16
BGLY17
BHOH206
BHOH224
BHOH225

site_idAC2
Number of Residues4
Detailsbinding site for residue SO4 A 101
ChainResidue
AARG8
AHOH204
AHOH217
ALYS7

site_idAC3
Number of Residues5
Detailsbinding site for residue SO4 A 102
ChainResidue
AMET36
AASN37
AHOH208
BPRO39
BGLY40

site_idAC4
Number of Residues3
Detailsbinding site for residue SO4 A 103
ChainResidue
AHIS69
ALYS70
BPRO1

site_idAC5
Number of Residues18
Detailsbinding site for residue K20 A 104
ChainResidue
AASP25
AGLY27
AALA28
AASP29
AASP30
AGLY48
AGLY49
AILE50
AVAL82
AHOH207
BASP25
BGLY27
BALA28
BASP30
BVAL32
BGLY48
BGLY49
BPRO81

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL
ChainResidueDetails
BALA22-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
ChainResidueDetails
BASP25
AASP25

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
BPHE99
APHE99

223532

PDB entries from 2024-08-07

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