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3O9A

Crystal Structure of wild-type HIV-1 Protease in complex with kd14

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
BGLY16
BHOH123
BHOH136
BHOH150

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 100
ChainResidue
ALYS70
AHOH110
BPRO1
AGLY68
AHIS69

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 B 101
ChainResidue
AMET36
AASN37
AHOH146
BPRO39
BGLY40
BHOH140

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 101
ChainResidue
ALYS20
AGLU21
AASN83
AHOH106
AHOH147

site_idAC5
Number of Residues18
DetailsBINDING SITE FOR RESIDUE K14 A 200
ChainResidue
AASP25
AGLY27
AALA28
AASP29
AASP30
AGLY48
AGLY49
AILE50
APRO81
AHOH114
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

222415

PDB entries from 2024-07-10

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