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6BZ2

Crystal structure of wild-type HIV-1 protease with a novel HIV-1 inhibitor GRL-14213A of 6-5-5-ring fused crown-like tetrahydropyranofuran as the P2-ligand, a cyclopropylaminobenzothiazole as the P2'-ligand and 3,5-difluorophenylmethyl as the 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
AHOH616
AHOH624
AHOH635
AHOH647
AHOH666

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

site_idAC3
Number of Residues33
Detailsbinding site for residue 7OA B 201
ChainResidue
AARG8
AASP25
AGLY27
AALA28
AASP29
AASP30
AVAL32
AILE47
AGLY48
AGLY49
AILE50
APRO81
AVAL82
AILE84
AHOH603
AHOH655
BARG8
BASP25
BGLY27
BALA28
BASP29
BASP30
BILE47
BGLY48
BGLY49
BILE50
BPRO81
BVAL82
BILE84
BHOH305
BHOH323
BHOH330
BHOH356

site_idAC4
Number of Residues1
Detailsbinding site for residue CL B 202
ChainResidue
BTRP6

site_idAC5
Number of Residues7
Detailsbinding site for residue ACT B 203
ChainResidue
BPRO39
BGLY40
BARG41
BTYR59
BASP60
BHOH316
BHOH333

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

237735

PDB entries from 2025-06-18

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