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6FH3

Protein arginine kinase McsB in the pArg-bound state

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0004111molecular_functioncreatine kinase activity
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0005615cellular_componentextracellular space
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
A0016775molecular_functionphosphotransferase activity, nitrogenous group as acceptor
A0046314biological_processphosphocreatine biosynthetic process
A1990424molecular_functionprotein arginine kinase activity
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0004111molecular_functioncreatine kinase activity
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0005615cellular_componentextracellular space
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
B0016775molecular_functionphosphotransferase activity, nitrogenous group as acceptor
B0046314biological_processphosphocreatine biosynthetic process
B1990424molecular_functionprotein arginine kinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue RPI A 401
ChainResidue
AVAL283
AHOH566
AHOH590
BGLN266
BHOH591
AASP285
ASER286
AGLU336
AARG338
AASP339
AARG342
AEDO406
AHOH531

site_idAC2
Number of Residues6
Detailsbinding site for residue EDO A 402
ChainResidue
AALA279
AARG282
AARG347
AARG351
AHOH576
AHOH587

site_idAC3
Number of Residues8
Detailsbinding site for residue EDO A 403
ChainResidue
AALA10
AVAL11
ASER12
AMET15
ALYS91
ALEU93
AGLU113
ALEU130

site_idAC4
Number of Residues3
Detailsbinding site for residue EDO A 405
ChainResidue
AALA137
AALA239
AHOH512

site_idAC5
Number of Residues2
Detailsbinding site for residue EDO A 406
ChainResidue
AGLU336
ARPI401

site_idAC6
Number of Residues10
Detailsbinding site for residue RPI B 401
ChainResidue
BASP285
BSER286
BPRO322
BPRO335
BARG338
BASP339
BARG342
BHOH507
BHOH511
BHOH521

site_idAC7
Number of Residues4
Detailsbinding site for residue EDO B 402
ChainResidue
BPHE272
BTYR275
BASN307
BHOH610

site_idAC8
Number of Residues6
Detailsbinding site for residue EDO B 403
ChainResidue
BARG86
BGLU213
BGLN321
BPRO322
BGLY323
BPHE324

site_idAC9
Number of Residues2
Detailsbinding site for residue EDO B 404
ChainResidue
BPHE61
BTRP149

Functional Information from PROSITE/UniProt
site_idPS00112
Number of Residues7
DetailsPHOSPHAGEN_KINASE Phosphagen kinase active site signature. CP.TNVGT
ChainResidueDetails
ACYS168-THR174

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues231
DetailsDomain: {"description":"Phosphagen kinase C-terminal"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues10
DetailsMotif: {"description":"RDXXRA motif of the pArg binding pocket involved in allosteric regulation","evidences":[{"source":"PubMed","id":"30962626","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"30962626","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00602","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00602","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"30962626","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

248335

PDB entries from 2026-01-28

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