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1M0B

HIV-1 protease in complex with an ethyleneamine inhibitor

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 0ZQ B 201
ChainResidue
AASP25
AILE50
APHE53
APRO81
AVAL82
AILE84
BASP125
BGLY127
BALA128
BASP129
BASP130
AGLY27
BILE147
BGLY148
BGLY149
BILE150
BPHE153
BPRO181
BVAL182
BILE184
BHOH401
BHOH402
AALA28
BHOH404
BHOH507
BHOH516
AASP29
AASP30
AVAL32
AILE47
AGLY48
AGLY49

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL B 701
ChainResidue
BTRP106
BHOH551

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
BASP125

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
APHE99
BPHE199

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
ATHR26
BTHR126
BASP125

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
BASP125

219140

PDB entries from 2024-05-01

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