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4MC1

HIV protease in complex with SA526P

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 Residues4
DetailsBINDING SITE FOR RESIDUE CL A 101
ChainResidue
ATHR74
AASN88
AHOH261
BARG41

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE 526 A 102
ChainResidue
AILE50
AILE84
AHOH295
BLEU23
BASP25
BGLY27
BALA28
BASP29
BASP30
BVAL32
BGLY49
BILE50
BHOH280
AASP25
AGLY27
AASP29
AASP30
AGLY49

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 101
ChainResidue
BTHR74
BASN88
BHOH225

site_idAC4
Number of Residues19
DetailsBINDING SITE FOR RESIDUE 526 B 102
ChainResidue
AASP25
AGLY27
AALA28
AASP29
AASP30
AVAL32
AILE50
BASP25
BGLY27
BALA28
BASP29
BASP30
BGLY48
BGLY49
BPRO81
BILE84
BHOH280
BHOH282
BHOH283

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 103
ChainResidue
BTRP6

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

222415

PDB entries from 2024-07-10

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