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4JDW

CRYSTAL STRUCTURE AND MECHANISM OF L-ARGININE: GLYCINE AMIDINOTRANSFERASE: A MITOCHONDRIAL ENZYME INVOLVED IN CREATINE BIOSYNTHESIS

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 PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ARG A 500
ChainResidue
AASP170
AGLY402
AALA407
AHOH601
AHOH634
AHOH658
AHOH668
AHOH688
AALA256
AMET302
AHIS303
AASP305
AALA306
AARG322
ASER354
ASER355

Functional Information from PROSITE/UniProt
site_idPS00430
Number of Residues98
DetailsTONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. mlrvrclrggsrgaeavhyigsrlgrtltgwvqrtfqstqaatassrnscaaddkateplpkdcpvssynewdpleevivgraenacvpp.........................FTIEVKAN
ChainResidueDetails
AMET1-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
AHIS303

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
AALA407

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:9218780, ECO:0007744|PDB:4JDW
ChainResidueDetails
AASP170
AASP305
AARG322
ASER354
ASER355

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

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS385

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1jdw
ChainResidueDetails
AASP254
AALA407
AHIS303

site_idMCSA1
Number of Residues5
DetailsM-CSA 18
ChainResidueDetails
AASP170electrostatic stabiliser, hydrogen bond acceptor
AASP254activator, electrostatic stabiliser, hydrogen bond acceptor
AHIS303hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AASP305electrostatic stabiliser, hydrogen bond acceptor
AALA407hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor

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PDB entries from 2024-11-13

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