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3LZU

Crystal Structure of a Nelfinavir Resistant HIV-1 CRF01_AE Protease variant (N88S) in Complex with the Protease 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 Residues5
DetailsBINDING SITE FOR RESIDUE ACT B 500
ChainResidue
ALEU63
AHOH107
AHOH129
BLYS70
BHOH129

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT B 100
ChainResidue
AARG8
BARG8

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT A 501
ChainResidue
ALYS70
BHOH124

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 100
ChainResidue
ALYS7
AARG8
BARG8

site_idAC5
Number of Residues26
DetailsBINDING SITE FOR RESIDUE 017 A 200
ChainResidue
AASP25
AGLY27
AALA28
AASP29
AASP30
AVAL32
AGLY48
AGLY49
AILE50
APRO81
AVAL82
AILE84
AHOH127
BASP25
BGLY27
BALA28
BASP29
BASP30
BVAL32
BGLY48
BGLY49
BILE50
BPRO81
BVAL82
BILE84
BHOH128

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 101
ChainResidue
AVAL11
ATHR12
ACYS67
BGLU65

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL
ChainResidueDetails
BALA22-LEU33

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI2
Number of Residues20
DetailsRegion: {"description":"Dimerization of protease","evidences":[{"source":"UniProtKB","id":"P04585","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"For protease activity; shared with dimeric partner","evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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