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2QI3

Crystal structure of protease inhibitor, MIT-2-AD94 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 Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 201
ChainResidue
AARG14
AGLY16
AGLY17
AHOH216
AHOH231
BGLY16
BHOH227
BHOH255

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 B 202
ChainResidue
AHIS69
ALYS70
AHOH238
BPRO1
BLYS55
AGLY68

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE MZ5 B 200
ChainResidue
AASP25
AGLY27
AALA28
AGLY48
AILE50
BASP25
BGLY27
BALA28
BASP30
BGLY48
BGLY49
BILE84
BHOH203
BHOH207
BHOH210

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

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
ATHR26

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
BASP25
BTHR26

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
BASP25

222926

PDB entries from 2024-07-24

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