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4ZLS

HIV-1 wild Type protease with GRL-096-13A (a Boc-derivative P2-Ligand, 3,-5-dimethylbiphenyl P1-Ligand)

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 Residues6
Detailsbinding site for residue NA A 501
ChainResidue
AASP60
AHOH620
AHOH626
AHOH634
AHOH640
AHOH654

site_idAC2
Number of Residues3
Detailsbinding site for residue CL A 502
ChainResidue
ATHR74
AASN88
BARG41

site_idAC3
Number of Residues2
Detailsbinding site for residue CL A 503
ChainResidue
AGLN18
ASER37

site_idAC4
Number of Residues19
Detailsbinding site for residue G61 B 201
ChainResidue
ATRP6
AASP25
AGLY27
AGLY48
AGLY49
AILE50
BLEU23
BASP25
BGLY27
BALA28
BASP29
BASP30
BGLY48
BGLY49
BPRO79
BPRO81
BVAL82
BILE84
BHOH302

site_idAC5
Number of Residues2
Detailsbinding site for residue CL B 202
ChainResidue
BTRP6
BHOH368

site_idAC6
Number of Residues5
Detailsbinding site for residue ACT B 203
ChainResidue
BPRO39
BARG41
BTYR59
BASP60
BHOH306

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, ECO:0000269|PubMed:12924029
ChainResidueDetails
AASP25
BASP25

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000269|PubMed:2476069
ChainResidueDetails
APHE99
BPHE99

222036

PDB entries from 2024-07-03

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