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1SP5

Crystal structure of HIV-1 protease complexed with a product of autoproteolysis

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 Residues2
DetailsBINDING SITE FOR RESIDUE CL A 601
ChainResidue
ATRP6
ALYS55

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 602
ChainResidue
ATHR74
AASN88
AHOH609

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 603
ChainResidue
AARG41
BTHR74
BASN88

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BME A 401
ChainResidue
ATHR12
ACYS67
AVAL11

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE BME B 402
ChainResidue
BCYS67

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BME A 403
ChainResidue
ATHR12
AGLU65
AGLY68
BSER37

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DMS A 501
ChainResidue
ALYS55
AVAL56
AARG57
AVAL77
AHOH667

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
BILE64

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by host => ECO:0000250
ChainResidueDetails
AILE64
BILE64

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
ATHR26
BASP25
BTHR26

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
BASP25

237992

PDB entries from 2025-06-25

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