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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6R8N

STRUCTURE DETERMINATION OF THE TETRAHEDRAL AMINOPEPTIDASE TET2 FROM P. HORIKOSHII BY USE OF COMBINED SOLID-STATE NMR, SOLUTION-STATE NMR AND EM DATA 4.1 A, FOLLOWED BY REAL_SPACE_REFINEMENT AT 4.1 A

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
B0004177molecular_functionaminopeptidase activity
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0008237molecular_functionmetallopeptidase activity
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
C0004177molecular_functionaminopeptidase activity
C0006508biological_processproteolysis
C0008233molecular_functionpeptidase activity
C0008237molecular_functionmetallopeptidase activity
C0016787molecular_functionhydrolase activity
C0046872molecular_functionmetal ion binding
D0004177molecular_functionaminopeptidase activity
D0006508biological_processproteolysis
D0008233molecular_functionpeptidase activity
D0008237molecular_functionmetallopeptidase activity
D0016787molecular_functionhydrolase activity
D0046872molecular_functionmetal ion binding
E0004177molecular_functionaminopeptidase activity
E0006508biological_processproteolysis
E0008233molecular_functionpeptidase activity
E0008237molecular_functionmetallopeptidase activity
E0016787molecular_functionhydrolase activity
E0046872molecular_functionmetal ion binding
F0004177molecular_functionaminopeptidase activity
F0006508biological_processproteolysis
F0008233molecular_functionpeptidase activity
F0008237molecular_functionmetallopeptidase activity
F0016787molecular_functionhydrolase activity
F0046872molecular_functionmetal ion binding
G0004177molecular_functionaminopeptidase activity
G0006508biological_processproteolysis
G0008233molecular_functionpeptidase activity
G0008237molecular_functionmetallopeptidase activity
G0016787molecular_functionhydrolase activity
G0046872molecular_functionmetal ion binding
H0004177molecular_functionaminopeptidase activity
H0006508biological_processproteolysis
H0008233molecular_functionpeptidase activity
H0008237molecular_functionmetallopeptidase activity
H0016787molecular_functionhydrolase activity
H0046872molecular_functionmetal ion binding
I0004177molecular_functionaminopeptidase activity
I0006508biological_processproteolysis
I0008233molecular_functionpeptidase activity
I0008237molecular_functionmetallopeptidase activity
I0016787molecular_functionhydrolase activity
I0046872molecular_functionmetal ion binding
J0004177molecular_functionaminopeptidase activity
J0006508biological_processproteolysis
J0008233molecular_functionpeptidase activity
J0008237molecular_functionmetallopeptidase activity
J0016787molecular_functionhydrolase activity
J0046872molecular_functionmetal ion binding
K0004177molecular_functionaminopeptidase activity
K0006508biological_processproteolysis
K0008233molecular_functionpeptidase activity
K0008237molecular_functionmetallopeptidase activity
K0016787molecular_functionhydrolase activity
K0046872molecular_functionmetal ion binding
L0004177molecular_functionaminopeptidase activity
L0006508biological_processproteolysis
L0008233molecular_functionpeptidase activity
L0008237molecular_functionmetallopeptidase activity
L0016787molecular_functionhydrolase activity
L0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 1001
ChainResidue
AHIS68
AASP182
AGLU213
AVAL236
site_idAC2
Number of Residues4
Detailsbinding site for residue ZN B 1001
ChainResidue
BHIS68
BASP182
BGLU213
BVAL236
site_idAC3
Number of Residues4
Detailsbinding site for residue ZN C 1001
ChainResidue
CASP182
CGLU213
CVAL236
CHIS68
site_idAC4
Number of Residues4
Detailsbinding site for residue ZN D 1001
ChainResidue
DHIS68
DASP182
DGLU213
DVAL236
site_idAC5
Number of Residues4
Detailsbinding site for residue ZN E 1001
ChainResidue
EHIS68
EASP182
EGLU213
EVAL236
site_idAC6
Number of Residues4
Detailsbinding site for residue ZN F 1001
ChainResidue
FHIS68
FASP182
FGLU213
FVAL236
site_idAC7
Number of Residues4
Detailsbinding site for residue ZN G 1001
ChainResidue
GHIS68
GASP182
GGLU213
GVAL236
site_idAC8
Number of Residues4
Detailsbinding site for residue ZN H 1001
ChainResidue
HHIS68
HASP182
HGLU213
HVAL236
site_idAC9
Number of Residues4
Detailsbinding site for residue ZN I 1001
ChainResidue
IHIS68
IASP182
IGLU213
IVAL236
site_idAD1
Number of Residues4
Detailsbinding site for residue ZN J 1001
ChainResidue
JHIS68
JASP182
JGLU213
JVAL236
site_idAD2
Number of Residues4
Detailsbinding site for residue ZN K 1001
ChainResidue
KHIS68
KASP182
KGLU213
KVAL236
site_idAD3
Number of Residues4
Detailsbinding site for residue ZN L 1001
ChainResidue
LHIS68
LASP182
LGLU213
LVAL236
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"15375159","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15713475","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues60
DetailsBinding site: {}
ChainResidueDetails

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PDB entries from 2026-01-28

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