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6UT6

Cryo-EM structure of the Escherichia coli McrBC complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003924molecular_functionGTPase activity
A0004519molecular_functionendonuclease activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005525molecular_functionGTP binding
A0009307biological_processDNA restriction-modification system
A0010385molecular_functiondouble-stranded methylated DNA binding
A0016887molecular_functionATP hydrolysis activity
A0042802molecular_functionidentical protein binding
A0044729molecular_functionhemi-methylated DNA-binding
A1905348cellular_componentendonuclease complex
B0003677molecular_functionDNA binding
B0003924molecular_functionGTPase activity
B0004519molecular_functionendonuclease activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005525molecular_functionGTP binding
B0009307biological_processDNA restriction-modification system
B0010385molecular_functiondouble-stranded methylated DNA binding
B0016887molecular_functionATP hydrolysis activity
B0042802molecular_functionidentical protein binding
B0044729molecular_functionhemi-methylated DNA-binding
B1905348cellular_componentendonuclease complex
C0003677molecular_functionDNA binding
C0003924molecular_functionGTPase activity
C0004519molecular_functionendonuclease activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005525molecular_functionGTP binding
C0009307biological_processDNA restriction-modification system
C0010385molecular_functiondouble-stranded methylated DNA binding
C0016887molecular_functionATP hydrolysis activity
C0042802molecular_functionidentical protein binding
C0044729molecular_functionhemi-methylated DNA-binding
C1905348cellular_componentendonuclease complex
D0003677molecular_functionDNA binding
D0003924molecular_functionGTPase activity
D0004519molecular_functionendonuclease activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005525molecular_functionGTP binding
D0009307biological_processDNA restriction-modification system
D0010385molecular_functiondouble-stranded methylated DNA binding
D0016887molecular_functionATP hydrolysis activity
D0042802molecular_functionidentical protein binding
D0044729molecular_functionhemi-methylated DNA-binding
D1905348cellular_componentendonuclease complex
E0003677molecular_functionDNA binding
E0003924molecular_functionGTPase activity
E0004519molecular_functionendonuclease activity
E0005515molecular_functionprotein binding
E0005524molecular_functionATP binding
E0005525molecular_functionGTP binding
E0009307biological_processDNA restriction-modification system
E0010385molecular_functiondouble-stranded methylated DNA binding
E0016887molecular_functionATP hydrolysis activity
E0042802molecular_functionidentical protein binding
E0044729molecular_functionhemi-methylated DNA-binding
E1905348cellular_componentendonuclease complex
F0003677molecular_functionDNA binding
F0003924molecular_functionGTPase activity
F0004519molecular_functionendonuclease activity
F0005515molecular_functionprotein binding
F0005524molecular_functionATP binding
F0005525molecular_functionGTP binding
F0009307biological_processDNA restriction-modification system
F0010385molecular_functiondouble-stranded methylated DNA binding
F0016887molecular_functionATP hydrolysis activity
F0042802molecular_functionidentical protein binding
F0044729molecular_functionhemi-methylated DNA-binding
F1905348cellular_componentendonuclease complex
G0005515molecular_functionprotein binding
G0009307biological_processDNA restriction-modification system
G0032067molecular_functiontype IV site-specific deoxyribonuclease activity
G1905348cellular_componentendonuclease complex
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue GDP A 501
ChainResidue
AASP176
ALEU177
APHE178
AGLY204
AGLY206
ALYS207
ATHR208
APHE209
ASER408

site_idAC2
Number of Residues17
Detailsbinding site for residue GSP B 501
ChainResidue
BASP176
BLEU177
BPHE178
BGLY204
BVAL205
BGLY206
BLYS207
BTHR208
BPHE209
BHIS407
BSER408
BMG502
CGLU298
CASP300
CLYS301
CARG348
CARG349

site_idAC3
Number of Residues4
Detailsbinding site for residue MG B 502
ChainResidue
BTHR208
BASP279
BGSP501
CARG349

site_idAC4
Number of Residues18
Detailsbinding site for residue GSP C 501
ChainResidue
CASP176
CLEU177
CPHE178
CGLY204
CVAL205
CGLY206
CLYS207
CTHR208
CPHE209
CASN333
CHIS407
CSER408
CMG502
DGLU298
DASP300
DLYS301
DARG348
DARG349

site_idAC5
Number of Residues3
Detailsbinding site for residue MG C 502
ChainResidue
CTHR208
CASP279
CGSP501

site_idAC6
Number of Residues19
Detailsbinding site for residue GSP D 501
ChainResidue
DASP176
DLEU177
DPHE178
DPRO203
DGLY204
DVAL205
DGLY206
DLYS207
DTHR208
DPHE209
DASN333
DHIS407
DSER408
DMG502
EGLU298
EASP300
ELYS301
EARG348
EARG349

site_idAC7
Number of Residues3
Detailsbinding site for residue MG D 502
ChainResidue
DTHR208
DASP279
DGSP501

site_idAC8
Number of Residues18
Detailsbinding site for residue GSP E 501
ChainResidue
EASP176
ELEU177
EPHE178
EGLY204
EVAL205
EGLY206
ELYS207
ETHR208
EPHE209
EASN333
EHIS407
ESER408
EMG502
FGLU298
FASP300
FLYS301
FARG348
FARG349

site_idAC9
Number of Residues3
Detailsbinding site for residue MG E 502
ChainResidue
ETHR208
EASP279
EGSP501

site_idAD1
Number of Residues11
Detailsbinding site for residue GSP F 501
ChainResidue
FGLY206
FLYS207
FTHR208
FPHE209
FHIS407
FSER408
AASP300
AARG348
FASP176
FPHE178
FGLY204

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AGLY201
DGLY201
DASP300
DASN333
EGLY201
EASP300
EASN333
FGLY201
FASP300
FASN333
AASP300
AASN333
BGLY201
BASP300
BASN333
CGLY201
CASP300
CASN333

222624

PDB entries from 2024-07-17

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