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1ZSF

Crystal Structure of Complex of a Hydroxyethylamine Inhibitor with HIV-1 Protease at 2.0A Resolution

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 Residues30
DetailsBINDING SITE FOR RESIDUE 0ZS B 201
ChainResidue
AASP25
AILE50
APHE53
APRO81
AVAL82
AILE84
BARG108
BASP125
BGLY127
BALA128
BASP129
AGLY27
BASP130
BILE147
BGLY148
BGLY149
BILE150
BPHE153
BVAL182
BILE184
BHOH301
BHOH327
AALA28
BHOH420
AASP29
AASP30
AVAL32
AILE47
AGLY48
AGLY49

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
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
AILE64
BILE164

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by host => ECO:0000250
ChainResidueDetails
AILE64
BILE164

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094, ECO:0000269|PubMed:12924029
ChainResidueDetails
AASP25
BASP125

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000269|PubMed:2476069
ChainResidueDetails
APHE99
BPHE199

218853

PDB entries from 2024-04-24

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