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5U92

Crystal Structure of arginine kinase from the spider Polybetes pythagoricus in complex with arginine

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
A0046314biological_processphosphocreatine biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue ARG A 401
ChainResidue
ASER63
AGLY64
AVAL65
AGLY66
ATYR68
AGLU225
ACYS271
AHOH557
AHOH566

site_idAC2
Number of Residues2
Detailsbinding site for residue NA A 402
ChainResidue
ATYR89
ALYS328

site_idAC3
Number of Residues2
Detailsbinding site for residue NA A 403
ChainResidue
AASP344
AGLU348

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:28924503, ECO:0007744|PDB:5U92
ChainResidueDetails
AGLY64
AGLU225
ACYS271

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00843
ChainResidueDetails
AARG229
AARG280
AARG309
ASER122
AHIS185

219869

PDB entries from 2024-05-15

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