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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

2BGN

HIV-1 Tat protein derived N-terminal nonapeptide Trp2-Tat(1-9) bound to the active site of Dipeptidyl peptidase IV (CD26)

Functional Information from GO Data
ChainGOidnamespacecontents
A0001618molecular_functionvirus receptor activity
A0001666biological_processresponse to hypoxia
A0002020molecular_functionprotease binding
A0004252molecular_functionserine-type endopeptidase activity
A0005102molecular_functionsignaling receptor binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005765cellular_componentlysosomal membrane
A0005886cellular_componentplasma membrane
A0005925cellular_componentfocal adhesion
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
A0008239molecular_functiondipeptidyl-peptidase activity
A0008240molecular_functiontripeptidyl-peptidase activity
A0008284biological_processpositive regulation of cell population proliferation
A0009986cellular_componentcell surface
A0010716biological_processnegative regulation of extracellular matrix disassembly
A0016020cellular_componentmembrane
A0016324cellular_componentapical plasma membrane
A0016486biological_processpeptide hormone processing
A0019065biological_processreceptor-mediated endocytosis of virus by host cell
A0030027cellular_componentlamellipodium
A0030139cellular_componentendocytic vesicle
A0031258cellular_componentlamellipodium membrane
A0031295biological_processT cell costimulation
A0033632biological_processregulation of cell-cell adhesion mediated by integrin
A0042110biological_processT cell activation
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0043542biological_processendothelial cell migration
A0045121cellular_componentmembrane raft
A0045499molecular_functionchemorepellent activity
A0046581cellular_componentintercellular canaliculus
A0046718biological_processsymbiont entry into host cell
A0046813biological_processreceptor-mediated virion attachment to host cell
A0050919biological_processnegative chemotaxis
A0061025biological_processmembrane fusion
A0070062cellular_componentextracellular exosome
A0070161cellular_componentanchoring junction
A0090024biological_processnegative regulation of neutrophil chemotaxis
A0120116biological_processglucagon processing
B0001618molecular_functionvirus receptor activity
B0001666biological_processresponse to hypoxia
B0002020molecular_functionprotease binding
B0004252molecular_functionserine-type endopeptidase activity
B0005102molecular_functionsignaling receptor binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005765cellular_componentlysosomal membrane
B0005886cellular_componentplasma membrane
B0005925cellular_componentfocal adhesion
B0006508biological_processproteolysis
B0008236molecular_functionserine-type peptidase activity
B0008239molecular_functiondipeptidyl-peptidase activity
B0008240molecular_functiontripeptidyl-peptidase activity
B0008284biological_processpositive regulation of cell population proliferation
B0009986cellular_componentcell surface
B0010716biological_processnegative regulation of extracellular matrix disassembly
B0016020cellular_componentmembrane
B0016324cellular_componentapical plasma membrane
B0016486biological_processpeptide hormone processing
B0019065biological_processreceptor-mediated endocytosis of virus by host cell
B0030027cellular_componentlamellipodium
B0030139cellular_componentendocytic vesicle
B0031258cellular_componentlamellipodium membrane
B0031295biological_processT cell costimulation
B0033632biological_processregulation of cell-cell adhesion mediated by integrin
B0042110biological_processT cell activation
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0043542biological_processendothelial cell migration
B0045121cellular_componentmembrane raft
B0045499molecular_functionchemorepellent activity
B0046581cellular_componentintercellular canaliculus
B0046718biological_processsymbiont entry into host cell
B0046813biological_processreceptor-mediated virion attachment to host cell
B0050919biological_processnegative chemotaxis
B0061025biological_processmembrane fusion
B0070062cellular_componentextracellular exosome
B0070161cellular_componentanchoring junction
B0090024biological_processnegative regulation of neutrophil chemotaxis
B0120116biological_processglucagon processing
C0001618molecular_functionvirus receptor activity
C0001666biological_processresponse to hypoxia
C0002020molecular_functionprotease binding
C0004252molecular_functionserine-type endopeptidase activity
C0005102molecular_functionsignaling receptor binding
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005765cellular_componentlysosomal membrane
C0005886cellular_componentplasma membrane
C0005925cellular_componentfocal adhesion
C0006508biological_processproteolysis
C0008236molecular_functionserine-type peptidase activity
C0008239molecular_functiondipeptidyl-peptidase activity
C0008240molecular_functiontripeptidyl-peptidase activity
C0008284biological_processpositive regulation of cell population proliferation
C0009986cellular_componentcell surface
C0010716biological_processnegative regulation of extracellular matrix disassembly
C0016020cellular_componentmembrane
C0016324cellular_componentapical plasma membrane
C0016486biological_processpeptide hormone processing
C0019065biological_processreceptor-mediated endocytosis of virus by host cell
C0030027cellular_componentlamellipodium
C0030139cellular_componentendocytic vesicle
C0031258cellular_componentlamellipodium membrane
C0031295biological_processT cell costimulation
C0033632biological_processregulation of cell-cell adhesion mediated by integrin
C0042110biological_processT cell activation
C0042802molecular_functionidentical protein binding
C0042803molecular_functionprotein homodimerization activity
C0043542biological_processendothelial cell migration
C0045121cellular_componentmembrane raft
C0045499molecular_functionchemorepellent activity
C0046581cellular_componentintercellular canaliculus
C0046718biological_processsymbiont entry into host cell
C0046813biological_processreceptor-mediated virion attachment to host cell
C0050919biological_processnegative chemotaxis
C0061025biological_processmembrane fusion
C0070062cellular_componentextracellular exosome
C0070161cellular_componentanchoring junction
C0090024biological_processnegative regulation of neutrophil chemotaxis
C0120116biological_processglucagon processing
D0001618molecular_functionvirus receptor activity
D0001666biological_processresponse to hypoxia
D0002020molecular_functionprotease binding
D0004252molecular_functionserine-type endopeptidase activity
D0005102molecular_functionsignaling receptor binding
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005765cellular_componentlysosomal membrane
D0005886cellular_componentplasma membrane
D0005925cellular_componentfocal adhesion
D0006508biological_processproteolysis
D0008236molecular_functionserine-type peptidase activity
D0008239molecular_functiondipeptidyl-peptidase activity
D0008240molecular_functiontripeptidyl-peptidase activity
D0008284biological_processpositive regulation of cell population proliferation
D0009986cellular_componentcell surface
D0010716biological_processnegative regulation of extracellular matrix disassembly
D0016020cellular_componentmembrane
D0016324cellular_componentapical plasma membrane
D0016486biological_processpeptide hormone processing
D0019065biological_processreceptor-mediated endocytosis of virus by host cell
D0030027cellular_componentlamellipodium
D0030139cellular_componentendocytic vesicle
D0031258cellular_componentlamellipodium membrane
D0031295biological_processT cell costimulation
D0033632biological_processregulation of cell-cell adhesion mediated by integrin
D0042110biological_processT cell activation
D0042802molecular_functionidentical protein binding
D0042803molecular_functionprotein homodimerization activity
D0043542biological_processendothelial cell migration
D0045121cellular_componentmembrane raft
D0045499molecular_functionchemorepellent activity
D0046581cellular_componentintercellular canaliculus
D0046718biological_processsymbiont entry into host cell
D0046813biological_processreceptor-mediated virion attachment to host cell
D0050919biological_processnegative chemotaxis
D0061025biological_processmembrane fusion
D0070062cellular_componentextracellular exosome
D0070161cellular_componentanchoring junction
D0090024biological_processnegative regulation of neutrophil chemotaxis
D0120116biological_processglucagon processing
E0004000molecular_functionadenosine deaminase activity
E0005515molecular_functionprotein binding
E0005737cellular_componentcytoplasm
E0005764cellular_componentlysosome
E0005829cellular_componentcytosol
E0005886cellular_componentplasma membrane
E0006154biological_processadenosine catabolic process
E0008270molecular_functionzinc ion binding
E0009168biological_processpurine ribonucleoside monophosphate biosynthetic process
E0009897cellular_componentexternal side of plasma membrane
E0019239molecular_functiondeaminase activity
E0042110biological_processT cell activation
E0043103biological_processhypoxanthine salvage
E0045187biological_processregulation of circadian sleep/wake cycle, sleep
E0046103biological_processinosine biosynthetic process
E0046936molecular_function2'-deoxyadenosine deaminase activity
E0060169biological_processnegative regulation of adenosine receptor signaling pathway
E0060205cellular_componentcytoplasmic vesicle lumen
E0070161cellular_componentanchoring junction
F0004000molecular_functionadenosine deaminase activity
F0005515molecular_functionprotein binding
F0005737cellular_componentcytoplasm
F0005764cellular_componentlysosome
F0005829cellular_componentcytosol
F0005886cellular_componentplasma membrane
F0006154biological_processadenosine catabolic process
F0008270molecular_functionzinc ion binding
F0009168biological_processpurine ribonucleoside monophosphate biosynthetic process
F0009897cellular_componentexternal side of plasma membrane
F0019239molecular_functiondeaminase activity
F0042110biological_processT cell activation
F0043103biological_processhypoxanthine salvage
F0045187biological_processregulation of circadian sleep/wake cycle, sleep
F0046103biological_processinosine biosynthetic process
F0046936molecular_function2'-deoxyadenosine deaminase activity
F0060169biological_processnegative regulation of adenosine receptor signaling pathway
F0060205cellular_componentcytoplasmic vesicle lumen
F0070161cellular_componentanchoring junction
G0004000molecular_functionadenosine deaminase activity
G0005515molecular_functionprotein binding
G0005737cellular_componentcytoplasm
G0005764cellular_componentlysosome
G0005829cellular_componentcytosol
G0005886cellular_componentplasma membrane
G0006154biological_processadenosine catabolic process
G0008270molecular_functionzinc ion binding
G0009168biological_processpurine ribonucleoside monophosphate biosynthetic process
G0009897cellular_componentexternal side of plasma membrane
G0019239molecular_functiondeaminase activity
G0042110biological_processT cell activation
G0043103biological_processhypoxanthine salvage
G0045187biological_processregulation of circadian sleep/wake cycle, sleep
G0046103biological_processinosine biosynthetic process
G0046936molecular_function2'-deoxyadenosine deaminase activity
G0060169biological_processnegative regulation of adenosine receptor signaling pathway
G0060205cellular_componentcytoplasmic vesicle lumen
G0070161cellular_componentanchoring junction
H0004000molecular_functionadenosine deaminase activity
H0005515molecular_functionprotein binding
H0005737cellular_componentcytoplasm
H0005764cellular_componentlysosome
H0005829cellular_componentcytosol
H0005886cellular_componentplasma membrane
H0006154biological_processadenosine catabolic process
H0008270molecular_functionzinc ion binding
H0009168biological_processpurine ribonucleoside monophosphate biosynthetic process
H0009897cellular_componentexternal side of plasma membrane
H0019239molecular_functiondeaminase activity
H0042110biological_processT cell activation
H0043103biological_processhypoxanthine salvage
H0045187biological_processregulation of circadian sleep/wake cycle, sleep
H0046103biological_processinosine biosynthetic process
H0046936molecular_function2'-deoxyadenosine deaminase activity
H0060169biological_processnegative regulation of adenosine receptor signaling pathway
H0060205cellular_componentcytoplasmic vesicle lumen
H0070161cellular_componentanchoring junction
Functional Information from PROSITE/UniProt
site_idPS00485
Number of Residues7
DetailsA_DEAMINASE Adenosine and AMP deaminase signature. SLNTDDP
ChainResidueDetails
ESER291-PRO297
site_idPS00708
Number of Residues31
DetailsPRO_ENDOPEP_SER Prolyl endopeptidase family serine active site. DqieAarqFskmgfvdnkriaiwGwSyGGYV
ChainResidueDetails
AASP605-VAL635
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU10084","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues8
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12483204","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12646248","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12906826","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20684603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23835475","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4L72","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20684603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23835475","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4L72","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12483204","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12906826","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20684603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23835475","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4L72","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12483204","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12646248","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20684603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23835475","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4L72","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12483204","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12646248","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12906826","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23835475","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4L72","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12483204","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12646248","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23835475","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4L72","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12483204","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20684603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23835475","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4L72","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues4
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P03958","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12554940","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14709046","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15139750","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15213224","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15239652","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15695814","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16033254","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16060665","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18549808","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KRM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NDV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NDW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NDY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NDZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O5R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QXL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1VFL","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12554940","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14709046","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15139750","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15239652","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16033254","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16060665","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18549808","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1NDW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NDY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NDZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O5R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QXL","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"14709046","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16060665","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1NDY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1WXY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12554940","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14709046","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15139750","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15239652","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16033254","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18549808","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1NDW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NDY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NDZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O5R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QXL","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues8
DetailsSite: {"description":"Important for interaction with adenosine receptors and increasing their affinity for agonists","evidences":[{"source":"UniProtKB","id":"P00813","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues4
DetailsSite: {"description":"Important for catalytic activity","evidences":[{"source":"UniProtKB","id":"P03958","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues8
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P00813","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a4l
ChainResidueDetails
EHIS238
ETYR240
EGLU217
EASP295
site_idCSA10
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a4l
ChainResidueDetails
BHIS740
BSER630
BASP709
site_idCSA11
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a4l
ChainResidueDetails
CHIS740
CSER630
CASP709
site_idCSA12
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a4l
ChainResidueDetails
DHIS740
DSER630
DASP709
site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a4l
ChainResidueDetails
FHIS238
FTYR240
FGLU217
FASP295
site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a4l
ChainResidueDetails
GHIS238
GTYR240
GGLU217
GASP295
site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a4l
ChainResidueDetails
HHIS238
HTYR240
HGLU217
HASP295
site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a4l
ChainResidueDetails
AHIS740
AASP708
ASER630
site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a4l
ChainResidueDetails
BHIS740
BASP708
BSER630
site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a4l
ChainResidueDetails
CHIS740
CASP708
CSER630
site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a4l
ChainResidueDetails
DHIS740
DASP708
DSER630
site_idCSA9
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a4l
ChainResidueDetails
AHIS740
ASER630
AASP709
site_idMCSA1
Number of Residues5
DetailsM-CSA 169
ChainResidueDetails
ATYR547electrostatic stabiliser, hydrogen bond donor
ASER630covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
ATYR631electrostatic stabiliser, hydrogen bond donor
AASP708activator, electrostatic stabiliser, hydrogen bond acceptor
AHIS740electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
site_idMCSA2
Number of Residues5
DetailsM-CSA 169
ChainResidueDetails
BTYR547electrostatic stabiliser, hydrogen bond donor
BSER630covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
BTYR631electrostatic stabiliser, hydrogen bond donor
BASP708activator, electrostatic stabiliser, hydrogen bond acceptor
BHIS740electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
site_idMCSA3
Number of Residues5
DetailsM-CSA 169
ChainResidueDetails
CTYR547electrostatic stabiliser, hydrogen bond donor
CSER630covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
CTYR631electrostatic stabiliser, hydrogen bond donor
CASP708activator, electrostatic stabiliser, hydrogen bond acceptor
CHIS740electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
site_idMCSA4
Number of Residues5
DetailsM-CSA 169
ChainResidueDetails
DTYR547electrostatic stabiliser, hydrogen bond donor
DSER630covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
DTYR631electrostatic stabiliser, hydrogen bond donor
DASP708activator, electrostatic stabiliser, hydrogen bond acceptor
DHIS740electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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PDB entries from 2026-04-01

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