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1V15

CRYSTAL STRUCTURE OF THE COLICIN E9, MUTANT HIS103ALA, IN COMPLEX WITH ZN+2 AND DSDNA (RESOLUTION 2.4A)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004519molecular_functionendonuclease activity
A0005102molecular_functionsignaling receptor binding
A0009617biological_processresponse to bacterium
A0019835biological_processcytolysis
B0004519molecular_functionendonuclease activity
B0005102molecular_functionsignaling receptor binding
B0009617biological_processresponse to bacterium
B0019835biological_processcytolysis
C0004519molecular_functionendonuclease activity
C0005102molecular_functionsignaling receptor binding
C0009617biological_processresponse to bacterium
C0019835biological_processcytolysis
D0004519molecular_functionendonuclease activity
D0005102molecular_functionsignaling receptor binding
D0009617biological_processresponse to bacterium
D0019835biological_processcytolysis
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A1132
ChainResidue
AHIS102
AHIS127
AHIS131
EDT5
EDC6

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B1135
ChainResidue
GDC6
BHIS102
BHIS127
BHIS131
GDT5

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN C1132
ChainResidue
CHIS102
CHIS127
CHIS131
IDT5
IDC6

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN D1135
ChainResidue
DHIS102
DHIS127
DHIS131
KDT5
KDC6

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN E1009
ChainResidue
EDG3
EHOH2004
LDG9
LDC10

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN G1009
ChainResidue
GDG3
GHOH2009
JDC10

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN I1009
ChainResidue
HDC10
IDG3
IHOH2006

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN K1009
ChainResidue
FDC10
KDG3

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues44
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues96
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues39
DetailsCompositional bias: {"description":"Low complexity","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 791
ChainResidueDetails
AARG5electrostatic stabiliser
AARG96electrostatic stabiliser
AGLU100electrostatic stabiliser
AHIS102metal ligand
AALA103increase nucleophilicity, proton acceptor, proton donor
AHIS127metal ligand
AHIS131metal ligand

site_idMCSA2
Number of Residues7
DetailsM-CSA 791
ChainResidueDetails
BARG5electrostatic stabiliser
BARG96electrostatic stabiliser
BGLU100electrostatic stabiliser
BHIS102metal ligand
BALA103increase nucleophilicity, proton acceptor, proton donor
BHIS127metal ligand
BHIS131metal ligand

site_idMCSA3
Number of Residues7
DetailsM-CSA 791
ChainResidueDetails
CARG5electrostatic stabiliser
CARG96electrostatic stabiliser
CGLU100electrostatic stabiliser
CHIS102metal ligand
CALA103increase nucleophilicity, proton acceptor, proton donor
CHIS127metal ligand
CHIS131metal ligand

site_idMCSA4
Number of Residues7
DetailsM-CSA 791
ChainResidueDetails
DARG5electrostatic stabiliser
DARG96electrostatic stabiliser
DGLU100electrostatic stabiliser
DHIS102metal ligand
DALA103increase nucleophilicity, proton acceptor, proton donor
DHIS127metal ligand
DHIS131metal ligand

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PDB entries from 2025-10-08

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