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3O99

Crystal Structure of wild-type HIV-1 Protease in complex with kd13

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 Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 100
ChainResidue
AARG14
AGLY16
AGLY17
AHOH127
AHOH133
AHOH134
BGLY16
BHOH118

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 B 100
ChainResidue
AASN37
AHOH136
BPRO39
BGLY40
BHOH124
AMET36

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT B 101
ChainResidue
AGLY68
AHIS69
ALYS70
BPRO1

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE K13 A 200
ChainResidue
AASP25
AGLY27
AALA28
AASP29
AASP30
AGLY48
AGLY49
AILE50
AHOH107
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

220472

PDB entries from 2024-05-29

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