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

1VRP

The 2.1 Structure of T. californica Creatine Kinase Complexed with the Transition-State Analogue Complex, ADP-Mg 2+ /NO3-/Creatine

Replaces:  1N16
Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004111molecular_functioncreatine kinase activity
A0005524molecular_functionATP binding
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0016301molecular_functionkinase activity
A0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
A0046314biological_processphosphocreatine biosynthetic process
B0003824molecular_functioncatalytic activity
B0004111molecular_functioncreatine kinase activity
B0005524molecular_functionATP binding
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0016301molecular_functionkinase activity
B0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
B0046314biological_processphosphocreatine biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 403
ChainResidue
BADP401
BNO3405
BHOH474
BHOH475
BHOH479
BHOH484

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 404
ChainResidue
AHOH461
AHOH462
AHOH463
AGLU232
AADP400
AHOH459

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NO3 B 405
ChainResidue
BGLU232
BARG236
BASN286
BARG320
BADP401
BIOM402
BMG403
BHOH469

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ADP A 400
ChainResidue
ASER128
AARG130
AARG132
AHIS191
ATRP228
AARG292
AGLY294
AVAL295
AHIS296
AARG320
ATHR322
AASP335
AMG404
AHOH446
AHOH458
AHOH459
AHOH462

site_idAC5
Number of Residues23
DetailsBINDING SITE FOR RESIDUE ADP B 401
ChainResidue
BSER128
BARG130
BARG132
BHIS191
BTRP228
BARG236
BARG292
BGLY294
BVAL295
BHIS296
BARG320
BTHR322
BGLY323
BGLY324
BVAL325
BASP335
BMG403
BNO3405
BHOH424
BHOH442
BHOH460
BHOH480
BHOH484

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE IOM B 402
ChainResidue
BILE69
BTHR71
BVAL72
BLEU201
BGLU232
BCYS283
BVAL325
BNO3405
BHOH426
BHOH462
BHOH481

Functional Information from PROSITE/UniProt
site_idPS00112
Number of Residues7
DetailsPHOSPHAGEN_KINASE Phosphagen kinase active site signature. CP.SNLGT
ChainResidueDetails
ACYS283-THR289

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING:
ChainResidueDetails
ASER128
AARG292
AARG320
AASP335
BSER128
BARG292
BARG320
BASP335

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00843
ChainResidueDetails
AHIS191
AARG236
BHIS191
BARG236

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1bg0
ChainResidueDetails
AARG236
AARG292
AARG320
AARG132
AGLU232

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1bg0
ChainResidueDetails
BARG236
BARG292
BARG320
BARG132
BGLU232

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon