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4EJD

HIV Protease (PR) dimer in closed form with pepstatin in active site and fragment 1F1 in the outside/top of flap

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 Residues7
DetailsBINDING SITE FOR RESIDUE BME A 101
ChainResidue
ALEU10
AVAL11
ATHR12
ACYS67
AHOH207
BLYS7
BHOH246

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 1F1 A 102
ChainResidue
ALYS55
AVAL56
AARG57
ATHR91
AGLN92
AGLY94
AHOH209
AHOH278
BHOH233
APRO44
ALYS45

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL B 101
ChainResidue
AGLY49
AGLY51
AGLY52
BPRO44
BMET46
BLYS55
BPRO81
BHOH225
BHOH251
CHOH104

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BME B 102
ChainResidue
ALYS7
AHOH227
BVAL11
BCYS67
BBME103

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BME B 103
ChainResidue
ALYS7
AHOH227
BTHR12
BCYS67
BBME102

site_idAC6
Number of Residues22
DetailsBINDING SITE FOR CHAIN C OF PEPSTATIN
ChainResidue
AARG8
AASP25
AGLY27
AALA28
AASP29
AASP30
ALYS45
AILE47
AGLY48
AGLY49
AILE84
BARG8
BASP25
BGLY27
BALA28
BASP29
BASP30
BGLY48
BHOH231
CHOH102
CHOH103
CHOH105

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
DetailsACT_SITE: For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094
ChainResidueDetails
AASP25
BASP25

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
APHE99
BPHE99

227344

PDB entries from 2024-11-13

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