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1Z1R

HIV-1 protease complexed with Macrocyclic peptidomimetic inhibitor 2

Replaces:  1B6O
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 SO4 B 501
ChainResidue
AGLY68
AHIS69
ALYS70
AHOH373
BPRO101
BLYS155

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 502
ChainResidue
APRO1
AHIS69

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 503
ChainResidue
AGLY17
AHOH390
BILE115
BGLY116
BGLY117
BHOH314
AARG14

site_idAC4
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HBH A 201
ChainResidue
AASP25
AGLY27
AALA28
AASP29
AASP30
AGLY48
AGLY49
AILE50
AVAL82
AHOH301
AHOH341
BARG108
BASP125
BGLY127
BALA128
BASP130
BGLY148
BGLY149
BVAL182
BILE184

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 Residues20
DetailsRegion: {"description":"Dimerization of protease","evidences":[{"source":"UniProtKB","id":"P04585","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"For protease activity; shared with dimeric partner","evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
ATHR26
BTHR126
BASP125

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
BASP125

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PDB entries from 2026-01-28

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