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1F7A

HOW DOES A SYMMETRIC DIMER RECOGNIZE AN ASYMMETRIC SUBSTRATE? A SUBSTRATE COMPLEX OF HIV-1 PROTEASE.

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 Residues4
DetailsBINDING SITE FOR RESIDUE ACT B 501
ChainResidue
APRO1
BGLY68
BHIS69
BLYS70

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT B 502
ChainResidue
AHOH526
BPRO1
BHIS69
BHOH528

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 504
ChainResidue
AARG8
AHOH538
ALYS7

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 506
ChainResidue
AGLY73
ATHR74
AASN88

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT B 507
ChainResidue
ALYS45
BGLN61
BHOH531
BHOH546
PLYS1
PALA2
PHOH12

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT B 508
ChainResidue
AARG14
APRO63
BARG14

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
AGLY78
BGLY78

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by host => ECO:0000250
ChainResidueDetails
AGLY78
BGLY78

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASN25
ATHR26
BASN25
BTHR26

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASN25
BASN25

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PDB entries from 2024-07-31

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