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2QI6

Crystal structure of protease inhibitor, MIT-2-KB98 in complex 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 Residues6
DetailsBINDING SITE FOR RESIDUE PO4 B 501
ChainResidue
AGLY68
AHIS69
ALYS70
AHOH551
BPRO1
BLYS55

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 502
ChainResidue
AHOH520
AHOH548
BGLY16
BHOH519
BHOH522
AARG14
AGLY16
AGLY17

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE MZ8 A 200
ChainResidue
AASP25
AGLY27
AALA28
AASP29
AASP30
AILE47
AGLY49
AILE50
AHOH508
BARG8
BASP25
BGLY27
BALA28
BASP30
BGLY48
BGLY49
BILE50
BPRO81
BILE84

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094
ChainResidueDetails
AASP25
BASP25

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
APHE99
BPHE99

218853

PDB entries from 2024-04-24

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