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2Q55

Crystal structure of KK44 bound to HIV-1 protease

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 Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 201
ChainResidue
AGLY68
AHIS69
ALYS70
AHOH231
BPRO1
BLYS55

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 202
ChainResidue
AHOH222
AHOH224
BGLY16
BHOH209
BHOH217
AARG14
AGLY16
AGLY17

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE MU0 B 200
ChainResidue
AASP25
AGLY27
AALA28
AASP29
AGLY48
AGLY49
BARG8
BASP25
BGLY27
BALA28
BASP29
BASP30
BILE47
BGLY48
BGLY49
BILE50
BVAL82
BHOH202
BHOH211
BHOH232
BHOH258

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

221051

PDB entries from 2024-06-12

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