Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3D1Z

Crystal structure of HIV-1 mutant I54M and inhibitor DARUNAVIR

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 Residues3
DetailsBINDING SITE FOR RESIDUE CL A 401
ChainResidue
ATHR74
AASN88
BARG41

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 601
ChainResidue
BTHR74
BASN88

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE 017 B 201
ChainResidue
AASP29
AASP30
AGLY48
AGLY49
AILE50
AILE84
BARG8
BASP25
BGLY27
BALA28
BASP29
BASP30
BGLY48
BGLY49
BILE50
BPRO81
BILE84
AARG8
AASP25
AGLY27
AALA28

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY B 301
ChainResidue
BPRO39
BGLY40
BARG41
BTYR59
BASP60

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

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon