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4BG4

Crystal structure of Litopenaeus vannamei arginine kinase in a ternary analog complex with arginine, ADP-Mg and NO3

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004054molecular_functionarginine kinase activity
A0004111molecular_functioncreatine kinase activity
A0005524molecular_functionATP binding
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
A0034618molecular_functionarginine binding
A0046072biological_processdTDP metabolic process
A0046314biological_processphosphocreatine biosynthetic process
B0003824molecular_functioncatalytic activity
B0004054molecular_functionarginine kinase activity
B0004111molecular_functioncreatine kinase activity
B0005524molecular_functionATP binding
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
B0034618molecular_functionarginine binding
B0046072biological_processdTDP metabolic process
B0046314biological_processphosphocreatine biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE ADP A 400
ChainResidue
ASER122
AVAL283
AHIS284
AARG309
ATHR311
AARG312
AGLY313
AGLU314
AASP324
ANO3405
AMG406
AARG124
AHOH2167
AHOH2233
AHOH2242
AHOH2297
AHOH2330
AARG126
AHIS185
ATRP221
AARG229
AMET233
AARG280
ASER282

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ARG A 403
ChainResidue
ASER63
AGLY64
AVAL65
AGLY66
ATYR68
AGLU225
ACYS271
AGLU314
ANO3405
AHOH2077
AHOH2091
AHOH2316

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE NO3 A 405
ChainResidue
AARG126
AGLU225
AARG229
AASN274
AARG309
AGLU314
AADP400
AARG403
AMG406
AHOH2295
AHOH2314

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 406
ChainResidue
AADP400
ANO3405
AHOH2272
AHOH2273
AHOH2314

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BME A 409
ChainResidue
ALEU46
AASP52
APRO138
ACYS139

site_idAC6
Number of Residues24
DetailsBINDING SITE FOR RESIDUE ADP B 400
ChainResidue
BSER122
BARG124
BARG126
BHIS185
BTRP221
BARG229
BMET233
BARG280
BSER282
BVAL283
BHIS284
BARG309
BTHR311
BARG312
BGLY313
BGLU314
BASP324
BNO3405
BMG407
BHOH2179
BHOH2185
BHOH2210
BHOH2213
BHOH2254

site_idAC7
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ARG B 403
ChainResidue
BSER63
BGLY64
BVAL65
BGLY66
BTYR68
BGLU225
BCYS271
BTHR273
BGLU314
BNO3405
BHOH2062
BHOH2076
BHOH2247

site_idAC8
Number of Residues10
DetailsBINDING SITE FOR RESIDUE NO3 B 405
ChainResidue
BADP400
BARG403
BMG407
BHOH2228
BARG126
BGLU225
BARG229
BASN274
BARG309
BGLU314

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BME B 406
ChainResidue
BASP52
BCYS139

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 407
ChainResidue
BADP400
BNO3405
BHOH2210
BHOH2211
BHOH2245

Functional Information from PROSITE/UniProt
site_idPS00112
Number of Residues7
DetailsPHOSPHAGEN_KINASE Phosphagen kinase active site signature. CP.TNLGT
ChainResidueDetails
ACYS271-THR277
BCYS271-THR277

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:23873077, ECO:0007744|PDB:4BG4, ECO:0007744|PDB:4BHL
ChainResidueDetails
BGLY64
BGLU225

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00843, ECO:0000269|PubMed:23873077, ECO:0007744|PDB:4BG4
ChainResidueDetails
BARG229
BARG280
BARG309
BSER122
BHIS185

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:23873077, ECO:0007744|PDB:4BG4
ChainResidueDetails
BGLU314
BCYS271

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PDB entries from 2024-05-15

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