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3R4B

Crystal Structure of Wild-type HIV-1 Protease in Complex With TMC310911

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 Residues27
DetailsBINDING SITE FOR RESIDUE 74T A 200
ChainResidue
AARG8
AILE50
APRO81
AVAL82
AILE84
AHOH109
BASP25
BGLY27
BALA28
BASP29
BASP30
ALEU23
BILE47
BGLY48
BGLY49
BILE50
BPRO81
BVAL82
BILE84
BHOH117
AASP25
AGLY27
AALA28
AASP29
AASP30
AGLY48
AGLY49

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 100
ChainResidue
AGLY16
AHOH126
AHOH140
AHOH141
BARG14
BGLY16
BGLY17

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL
ChainResidueDetails
AALA22-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
AASP25
BASP25

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

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PDB entries from 2024-10-09

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