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2QMP

Crystal Structure of HIV-1 protease complexed with PL-100

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 Residues21
DetailsBINDING SITE FOR RESIDUE A00 A 100
ChainResidue
ATRP6
AILE84
AHOH124
BARG8
BASP25
BALA28
BASP30
BGLY48
BGLY49
BILE50
BPRO81
AASP25
BILE84
BHOH135
AGLY27
AALA28
AASP29
AILE47
AGLY48
AGLY49
AILE50

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE A00 B 100
ChainResidue
AARG8
AASP25
AALA28
AASP30
AGLY48
AGLY49
AILE50
AHOH124
BASP25
BGLY27
BALA28
BASP29
BILE47
BGLY48
BILE50
BHOH158
BHOH217

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL
ChainResidueDetails
AALA22-LEU33

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
ATHR26

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
BASP25
BTHR26

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
BASP25

237735

PDB entries from 2025-06-18

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