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4HDB

Crystal Structure of HIV-1 protease mutants D30N 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 Residues29
DetailsBINDING SITE FOR RESIDUE G52 A 401
ChainResidue
AARG8
APRO81
AVAL82
AILE84
AHOH1001
AHOH1002
AHOH1092
AHOH1093
BASP125
BGLY127
BALA128
AASP25
BASP129
BASN130
BVAL132
BGLY148
BGLY149
BILE150
BPRO181
BVAL182
BHOH307
BHOH383
AGLY27
AALA28
AASP29
AASN30
AGLY48
AGLY49
AILE50

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 402
ChainResidue
AASP60
AHOH1003
AHOH1004
AHOH1005
AHOH1006
AHOH1007

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 403
ChainResidue
ATHR74
AASN88
AHOH1074
BARG141

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 201
ChainResidue
BTRP106

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADNTVI
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
BASP125

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
APHE99
BPHE199

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PDB entries from 2024-10-16

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