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

2JDX

CRYSTAL STRUCTURE OF HUMAN L-ARGININE:GLYCINE AMIDINOTRANSFERASE, DELETIONMUTANT ATDELTAM302

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0005758cellular_componentmitochondrial intermembrane space
A0006600biological_processcreatine metabolic process
A0006601biological_processcreatine biosynthetic process
A0007611biological_processlearning or memory
A0014889biological_processmuscle atrophy
A0015067molecular_functionamidinotransferase activity
A0015068molecular_functionglycine amidinotransferase activity
A0016740molecular_functiontransferase activity
A0070062cellular_componentextracellular exosome
A0120162biological_processpositive regulation of cold-induced thermogenesis
Functional Information from PROSITE/UniProt
site_idPS00430
Number of Residues61
DetailsTONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. stqaatassrnscaaddkateplpkdcpvssynewdpleevivgraenacvpp..............................................................FTIEVKAN
ChainResidueDetails
ASER38-ASN98

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:9218780, ECO:0007744|PDB:4JDW
ChainResidueDetails
AASP254
AILE304

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Amidino-cysteine intermediate => ECO:0000269|PubMed:9148748, ECO:0000269|PubMed:9218780, ECO:0007744|PDB:4JDW
ChainResidueDetails
ATRP408

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:9218780, ECO:0007744|PDB:4JDW
ChainResidueDetails
APRO323
ASER355
ALYS356
AASP170
AALA306

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER49
ASER46

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALEU386

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 18
ChainResidueDetails
AASP170electrostatic stabiliser, hydrogen bond acceptor
AASP254activator, electrostatic stabiliser, hydrogen bond acceptor
AILE304hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AALA306electrostatic stabiliser, hydrogen bond acceptor
ATRP408hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon