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2I0A

Crystal Structure of KB-19 complexed with wild type 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 Residues8
DetailsBINDING SITE FOR RESIDUE PO4 B 501
ChainResidue
AARG14
AGLY16
AGLY17
AHOH622
AHOH665
BGLY16
BHOH525
BHOH559

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 B 503
ChainResidue
AHIS69
ALYS70
AHOH625
BPRO1
BHOH577
AGLY68

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 504
ChainResidue
AMET36
AASN37
AHOH670
BPRO39
BGLY40
BHOH514

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 505
ChainResidue
ALYS20
AGLU21
AASN83
AHOH637
AHOH659
AHOH664

site_idAC5
Number of Residues19
DetailsBINDING SITE FOR RESIDUE MUI A 200
ChainResidue
AASP25
AGLY27
AALA28
AASP29
AGLY48
AILE50
AVAL82
AGOL601
AHOH604
AHOH641
BARG8
BASP25
BGLY27
BALA28
BASP30
BGLY48
BGLY49
BVAL82
BILE84

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 601
ChainResidue
AGLY49
APHE53
AMUI200
AHOH644
AHOH661
BTHR91
BGLN92
BHOH554

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 Residues4
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
ATHR26
BASP25
BTHR26

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
BASP25

222624

PDB entries from 2024-07-17

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