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4F75

Crystal Structure of active HIV-1 Protease in Complex with the N terminal product of the substrate RH-IN

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 GOL A 101
ChainResidue
AARG14
AGLY16
AGLY17
AHOH235
BARG14
BGLY17
BHOH107
BHOH134

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 102
ChainResidue
AARG8
AHOH225
ALYS7

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR CHAIN C OF N TERMINAL PRODUCT OF SUBSTRATE RH-IN
ChainResidue
AASP25
AGLY27
AALA28
AASP29
AASP30
AGLY48
AGLY49
APHE53
BARG8
BASP25
BILE50
BVAL82
CHOH101
CHOH102
CHOH103
DPHE6

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR CHAIN D OF C TERMINAL PRODUCT OF SUBSTRATE RH-IN
ChainResidue
AASP25
APRO81
AILE84
BGLY27
BALA28
BASP29
BASP30
BVAL32
BGLY48
BILE50
BILE84
CLEU5
CHOH103

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

222415

PDB entries from 2024-07-10

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