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6HZ4

Structure of McrBC without DNA binding domains (one half of the full complex)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0016887molecular_functionATP hydrolysis activity
B0005524molecular_functionATP binding
B0016887molecular_functionATP hydrolysis activity
C0005524molecular_functionATP binding
C0016887molecular_functionATP hydrolysis activity
D0005524molecular_functionATP binding
D0016887molecular_functionATP hydrolysis activity
E0005524molecular_functionATP binding
E0016887molecular_functionATP hydrolysis activity
F0005524molecular_functionATP binding
F0016887molecular_functionATP hydrolysis activity
M0005515molecular_functionprotein binding
M0009307biological_processDNA restriction-modification system
M0032067molecular_functiontype IV site-specific deoxyribonuclease activity
M1905348cellular_componentendonuclease complex
N0005515molecular_functionprotein binding
N0009307biological_processDNA restriction-modification system
N0032067molecular_functiontype IV site-specific deoxyribonuclease activity
N1905348cellular_componentendonuclease complex
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue GNP A 1001
ChainResidue
AASP176
AGLU280
AHIS407
ASER408
AMG1002
BASP300
BLYS301
BALA345
BARG348
BARG349
ALEU177
APHE178
APRO203
AGLY204
AGLY206
ALYS207
ATHR208
APHE209

site_idAC2
Number of Residues3
Detailsbinding site for residue MG A 1002
ChainResidue
ATHR208
AASP279
AGNP1001

site_idAC3
Number of Residues19
Detailsbinding site for residue GNP B 1001
ChainResidue
BASP176
BLEU177
BPHE178
BPRO203
BGLY204
BGLY206
BLYS207
BTHR208
BPHE209
BGLU280
BHIS407
BSER408
BCYS411
BCYS412
BMG1002
CASP300
CLYS301
CARG348
CARG349

site_idAC4
Number of Residues3
Detailsbinding site for residue MG B 1002
ChainResidue
BTHR208
BASP279
BGNP1001

site_idAC5
Number of Residues20
Detailsbinding site for residue GNP C 1001
ChainResidue
CASP176
CLEU177
CPHE178
CPRO202
CPRO203
CGLY204
CVAL205
CGLY206
CLYS207
CTHR208
CPHE209
CHIS407
CSER408
CCYS411
CCYS412
CMG1002
DASP300
DLYS301
DALA345
DARG349

site_idAC6
Number of Residues3
Detailsbinding site for residue MG C 1002
ChainResidue
CTHR208
CASP279
CGNP1001

site_idAC7
Number of Residues12
Detailsbinding site for residue GDP D 1001
ChainResidue
DASP176
DPHE178
DPRO203
DGLY204
DVAL205
DGLY206
DLYS207
DTHR208
DPHE209
DHIS407
DSER408
DCYS411

site_idAC8
Number of Residues15
Detailsbinding site for residue GDP E 1001
ChainResidue
EASP176
EPHE178
EPRO203
EGLY204
EVAL205
EGLY206
ELYS207
ETHR208
EPHE209
EHIS407
ESER408
ECYS411
FGLU298
FASP300
FARG348

site_idAC9
Number of Residues10
Detailsbinding site for residue GDP F 1001
ChainResidue
FPHE209
FHIS407
FSER408
FCYS411
ALYS301
AARG348
FPHE178
FGLY206
FLYS207
FTHR208

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
APRO362
BPRO362
CPRO362
DPRO362
EPRO362
FPRO362

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PDB entries from 2024-07-10

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