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4RF7

Crystal structure of double-domain arginine kinase from Anthopleura japonicas in complex with substrate L-arginine

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0004054molecular_functionarginine kinase activity
A0004111molecular_functioncreatine kinase activity
A0005524molecular_functionATP binding
A0005615cellular_componentextracellular space
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
A0046314biological_processphosphocreatine biosynthetic process
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0004054molecular_functionarginine kinase activity
B0004111molecular_functioncreatine kinase activity
B0005524molecular_functionATP binding
B0005615cellular_componentextracellular space
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
B0046314biological_processphosphocreatine biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 801
ChainResidue
AHIS455
ATHR456
ASER457
AHIS617
AHOH987

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 802
ChainResidue
AHOH975
ASER420
ACYS421
AGLY422
ATYR424

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT A 803
ChainResidue
AMET459
AARG807

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ARG A 805
ChainResidue
ASER67
AGLY68
AVAL69
AGLY70
ATYR72
AGLU229
ACYS275
AHOH913
AHOH1002
AHOH1154

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ARG A 806
ChainResidue
ASER126
AARG128
AARG284
ASER286
AHIS288
AHOH1267

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ARG A 807
ChainResidue
ALYS488
AASP610
AGLY614
APHE615
ATYR623
AACT803
AHOH1094
AHOH1173

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT B 1001
ChainResidue
BARG480
BARG482
BARG585

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT B 1002
ChainResidue
BHIS308
BGLN343
BASP347

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT B 1003
ChainResidue
BARG128
BARG130
BARG233
BARG284

site_idBC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ARG B 1005
ChainResidue
BSER67
BGLY68
BVAL69
BGLY70
BTYR72
BGLU229
BCYS275
BSER277
BHOH1119
BHOH1144
BHOH1226
BHOH1284

site_idBC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ARG B 1006
ChainResidue
BSER126
BTHR127
BARG128
BMET237
BLYS239
BSER286
BHIS288
BHOH1151
BHOH1511
BHOH1600

site_idBC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ARG B 1007
ChainResidue
BARG122
BASP408
BASN411
BPRO494
BALA553
BALA554
BGLY555
BLYS558
BHOH1193
BHOH1353
BHOH1410

Functional Information from PROSITE/UniProt
site_idPS00112
Number of Residues7
DetailsPHOSPHAGEN_KINASE Phosphagen kinase active site signature. CP.SNLGT
ChainResidueDetails
ACYS275-THR281
ACYS627-THR633

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLY68
AGLU229
ACYS275
AGLU317
BGLY68
BGLU229
BCYS275
BGLU317

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00843
ChainResidueDetails
ASER126
BARG312
AHIS189
AARG233
AARG284
AARG312
BSER126
BHIS189
BARG233
BARG284

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PDB entries from 2025-06-25

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