Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6U7B

Structure of E. coli MS115-1 CdnC:HORMA-deltaN complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0001730molecular_function2'-5'-oligoadenylate synthetase activity
A0003725molecular_functiondouble-stranded RNA binding
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0009117biological_processnucleotide metabolic process
A0016020cellular_componentmembrane
A0016740molecular_functiontransferase activity
A0016779molecular_functionnucleotidyltransferase activity
A0046872molecular_functionmetal ion binding
A0051607biological_processdefense response to virus
A0106408molecular_functiondiadenylate cyclase activity
B0051607biological_processdefense response to virus
C0000166molecular_functionnucleotide binding
C0001730molecular_function2'-5'-oligoadenylate synthetase activity
C0003725molecular_functiondouble-stranded RNA binding
C0005524molecular_functionATP binding
C0005829cellular_componentcytosol
C0009117biological_processnucleotide metabolic process
C0016020cellular_componentmembrane
C0016740molecular_functiontransferase activity
C0016779molecular_functionnucleotidyltransferase activity
C0046872molecular_functionmetal ion binding
C0051607biological_processdefense response to virus
C0106408molecular_functiondiadenylate cyclase activity
D0051607biological_processdefense response to virus
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue MG A 401
ChainResidue
AASP72
AASP74
AHOH503

site_idAC2
Number of Residues5
Detailsbinding site for residue CL A 402
ChainResidue
AGLY59
ASER60
ALEU61
AASP74
AHOH532

site_idAC3
Number of Residues5
Detailsbinding site for residue ACT B 201
ChainResidue
BASP153
BLYS154
BACT202
BHOH333
BASP93

site_idAC4
Number of Residues4
Detailsbinding site for residue ACT B 202
ChainResidue
BASP93
BASN152
BTHR155
BACT201

site_idAC5
Number of Residues4
Detailsbinding site for residue ACT B 203
ChainResidue
BARG99
BTYR149
BGLU151
DTYR149

site_idAC6
Number of Residues6
Detailsbinding site for residue MG C 401
ChainResidue
CASP72
CASP74
CHOH506
CHOH518
CHOH540
CHOH600

site_idAC7
Number of Residues11
Detailsbinding site for residue AMP C 402
ChainResidue
CSER58
CLYS63
CLEU155
CHIS162
CLYS201
CSER202
CPHE203
CASN270
CVAL272
CHOH522
CHOH552

site_idAC8
Number of Residues4
Detailsbinding site for residue CL C 403
ChainResidue
CSER60
CLEU61
CASP74
CHOH543

site_idAC9
Number of Residues3
Detailsbinding site for residue ACT D 201
ChainResidue
DASP93
DLYS97
DLYS154

site_idAD1
Number of Residues3
Detailsbinding site for residue ACT D 202
ChainResidue
DASP93
DASN152
DTHR155

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:31932165, ECO:0007744|PDB:6P80, ECO:0007744|PDB:6P8V
ChainResidueDetails
APRO48
AILE147
ALYS170
ATYR186
CPRO48
CILE147
CLYS170
CTYR186

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:31932165, ECO:0007744|PDB:6U7B
ChainResidueDetails
APRO57
CPRO57

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:31932165, ECO:0007744|PDB:6P80, ECO:0007744|PDB:6P8V, ECO:0007744|PDB:6U7B
ChainResidueDetails
AGLY59
CGLY59

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:31932165, ECO:0007744|PDB:6P80
ChainResidueDetails
ATHR255
CTHR255

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon