Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6HP8

Crystal structure of DPP8 in complex with Val-BoroPro

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0006915biological_processapoptotic process
A0006955biological_processimmune response
A0008236molecular_functionserine-type peptidase activity
A0008239molecular_functiondipeptidyl-peptidase activity
A0043069biological_processnegative regulation of programmed cell death
B0004177molecular_functionaminopeptidase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006508biological_processproteolysis
B0006915biological_processapoptotic process
B0006955biological_processimmune response
B0008236molecular_functionserine-type peptidase activity
B0008239molecular_functiondipeptidyl-peptidase activity
B0043069biological_processnegative regulation of programmed cell death
C0004177molecular_functionaminopeptidase activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006508biological_processproteolysis
C0006915biological_processapoptotic process
C0006955biological_processimmune response
C0008236molecular_functionserine-type peptidase activity
C0008239molecular_functiondipeptidyl-peptidase activity
C0043069biological_processnegative regulation of programmed cell death
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue GK2 A 901
ChainResidue
AARG160
AASN835
AHIS865
AGLU275
AGLU276
ATYR669
AGLN673
ASER755
ATYR756
ATYR787
ATYR791

site_idAC2
Number of Residues5
Detailsbinding site for residue NA A 902
ChainResidue
AARG158
AGLN274
AGLU275
AASP278
ATYR280

site_idAC3
Number of Residues7
Detailsbinding site for residue GOL A 903
ChainResidue
AHIS315
ATHR317
AARG324
AALA326
APHE831
AHIS837
AHOH1083

site_idAC4
Number of Residues5
Detailsbinding site for residue GOL A 904
ChainResidue
AHIS188
ALEU206
AGLU208
AILE241
AHOH1003

site_idAC5
Number of Residues9
Detailsbinding site for residue GOL A 905
ChainResidue
AGLY526
ASER527
AASN528
AILE529
AGLN530
AGLU541
ACYS575
AILE577
AHOH1014

site_idAC6
Number of Residues7
Detailsbinding site for residue GOL A 906
ChainResidue
AASN448
AHIS525
AGLN673
AHOH1031
AHOH1102
AHOH1166
AHOH1201

site_idAC7
Number of Residues6
Detailsbinding site for residue GOL A 907
ChainResidue
ATRP383
ATHR384
APRO385
ATRP391
APHE453
AVAL455

site_idAC8
Number of Residues5
Detailsbinding site for residue NA B 902
ChainResidue
BARG158
BGLN274
BASP278
BTYR280
BHOH1131

site_idAC9
Number of Residues6
Detailsbinding site for residue GOL B 903
ChainResidue
BTHR317
BARG324
BARG325
CHIS315
CHIS837
CGOL903

site_idAD1
Number of Residues6
Detailsbinding site for residue GOL B 904
ChainResidue
AHOH1011
BHIS188
BLEU206
BGLU208
BILE241
BARG244

site_idAD2
Number of Residues6
Detailsbinding site for residue GOL B 905
ChainResidue
BTRP383
BTRP391
BPHE453
BHIS454
BVAL455
BHOH1002

site_idAD3
Number of Residues7
Detailsbinding site for residue GOL B 906
ChainResidue
BASN448
BILE449
BARG524
BGLN673
BARG794
BHOH1025
BHOH1051

site_idAD4
Number of Residues8
Detailsbinding site for residue GOL B 907
ChainResidue
BGLY526
BSER527
BASN528
BGLN530
BGLU541
BCYS575
BILE577
BHOH1174

site_idAD5
Number of Residues5
Detailsbinding site for residue NA C 902
ChainResidue
CARG158
CGLN274
CASP278
CTYR280
CHOH1007

site_idAD6
Number of Residues8
Detailsbinding site for residue GOL C 903
ChainResidue
CALA326
CPHE831
BHIS315
BHIS837
BGOL903
BHOH1115
CTHR317
CARG324

site_idAD7
Number of Residues5
Detailsbinding site for residue GOL C 904
ChainResidue
CTRP383
CTRP391
CPHE453
CHIS454
CVAL455

site_idAD8
Number of Residues10
Detailsbinding site for residue GOL C 905
ChainResidue
CASN448
CARG524
CHIS525
CGLN673
CARG794
CHOH1004
CHOH1030
CHOH1067
CHOH1123
CHOH1166

site_idAD9
Number of Residues6
Detailsbinding site for residue GOL C 906
ChainResidue
CGLY526
CSER527
CASN528
CGLU541
CCYS575
CILE577

site_idAE1
Number of Residues2
Detailsbinding site for residue GOL C 907
ChainResidue
CHIS595
CLYS682

site_idAE2
Number of Residues17
Detailsbinding site for Di-peptide GK2 B 901 and SER B 755
ChainResidue
BARG160
BGLU275
BGLU276
BTYR669
BGLN673
BTRP754
BTYR756
BGLY757
BGLY758
BTYR759
BGLY778
BALA779
BPRO780
BTYR787
BTYR791
BASN835
BHIS865

site_idAE3
Number of Residues17
Detailsbinding site for Di-peptide GK2 C 901 and SER C 755
ChainResidue
CARG160
CGLU275
CGLU276
CTYR669
CGLN673
CTRP754
CTYR756
CGLY757
CGLY758
CTYR759
CGLY778
CALA779
CTYR787
CTYR791
CASN835
CHIS865
CHOH1150

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsACT_SITE: Charge relay system => ECO:0000305|PubMed:12534281, ECO:0000305|PubMed:29382749
ChainResidueDetails
ASER755
AASP833
AHIS865
BSER755
BASP833
BHIS865
CSER755
CASP833
CHIS865

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon