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4HE9

Crystal Structure of HIV-1 protease mutants I54M complexed with inhibitor GRL-0519

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 Residues31
DetailsBINDING SITE FOR RESIDUE G52 A 401
ChainResidue
AASP25
AVAL82
AILE84
AHOH552
AHOH561
AHOH583
AHOH593
BARG8
BLEU23
BASP25
BGLY27
AGLY27
BALA28
BASP29
BASP30
BGLY48
BGLY49
BILE50
BPRO81
BVAL82
BILE84
BHOH253
AALA28
BHOH290
BHOH293
AASP29
AASP30
AGLY48
AGLY49
AILE50
APRO81

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 402
ChainResidue
AASP60
AHOH528
AHOH529
AHOH530
AHOH531
AHOH532

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 403
ChainResidue
ATHR74
AASN88
AHOH592
AHOH599
BARG41

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CL A 404
ChainResidue
ATHR26
AGLY27
AASP29
AARG87
AHOH519
BARG8
BPRO9
BLEU23

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 101
ChainResidue
BTRP6

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 102
ChainResidue
BTHR74
BASN88
BHOH231

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CL B 103
ChainResidue
AARG8
APRO9
BTHR26
BGLY27
BASP29
BARG87
BHOH229

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVI
ChainResidueDetails
AALA22-ILE33

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

221051

PDB entries from 2024-06-12

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