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4MC6

HIV protease in complex with SA499

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 Residues32
DetailsBINDING SITE FOR RESIDUE 23K A 101
ChainResidue
AARG8
AILE50
APRO81
AVAL82
AILE84
AHOH266
AHOH271
AHOH306
AHOH321
AHOH323
BARG8
ALEU23
BLEU23
BASP25
BGLY27
BALA28
BASP29
BASP30
BILE47
BGLY48
BGLY49
BILE50
AASP25
BVAL82
BILE84
BHOH231
AGLY27
AALA28
AASP29
AASP30
AGLY48
AGLY49

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 102
ChainResidue
AGLN18
AMET36
ASER37
BTHR12
BGLU65
BCYS67
BGLY68

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 103
ChainResidue
ATHR74
AASN88
AHOH252
BARG41

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 101
ChainResidue
BTRP6

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 102
ChainResidue
BTHR74
BASN88
BHOH226

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
BASP25

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

218853

PDB entries from 2024-04-24

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