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3O9D

Crystal Structure of wild-type HIV-1 Protease in complex with kd19

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 Residues7
DetailsBINDING SITE FOR RESIDUE PO4 B 100
ChainResidue
AARG14
AGLY16
AGLY17
AHOH145
BGLY16
BHOH122
BHOH123

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 100
ChainResidue
AASN83
AHOH120
BHOH131
ALYS20
AGLU21

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 101
ChainResidue
AHIS69
ALYS70
BPRO1

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 102
ChainResidue
AMET36
AASN37
AHOH146
BPRO39
BGLY40

site_idAC5
Number of Residues18
DetailsBINDING SITE FOR RESIDUE K19 A 200
ChainResidue
AASP25
AGLY27
AALA28
AASP29
AASP30
AGLY48
AGLY49
AILE50
APRO81
AHOH127
BASP25
BGLY27
BALA28
BASP30
BGLY48
BGLY49
BVAL82
BILE84

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

225946

PDB entries from 2024-10-09

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