Structure of PDB 1jdx Chain A

Receptor sequence
>1jdxA (length=360) Species: 9606 (Homo sapiens) [Search protein sequence]
CPVSSYNEWDPLEEVIVGRAENACVPPFTIEVKANTYEKYWPFYQKQGGH
YFPKDHLKKAVAEIEEMCNILKTEGVTVRRPDPIDWSLKYKTPDFESTGL
YSAMPRDILIVVGNEIIEAPMAWRSRFFEYRAYRSIIKDYFHRGAKWTTA
PKPTMADELYNQDYPIHSVEDRHKLAAQGKFVTTEFEPCFDAADFIRAGR
DIFAQRSQVTNYLGIEWMRRHLAPDYRVHIISFKDPNPMHIDATFNIIGP
GIVLSNPDRPCHQIDLFKKAGWTIITPPTPIIPDDHPLWMSSKWLSMNVL
MLDEKRVMVDANEVPIQKMFEKLGITTIKVNIRNANSLGGGFHCWTCDVR
RRGTLQSYLD
3D structure
PDB1jdx The ligand-induced structural changes of human L-Arginine:Glycine amidinotransferase. A mutational and crystallographic study.
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E71 D170 D254 H303 D305 N361 H406 C407
Catalytic site (residue number reindexed from 1) E8 D107 D191 H240 D242 N298 H343 C344
Enzyme Commision number 2.1.4.1: glycine amidinotransferase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 NVA A M302 A306 R322 S354 S355 M239 A243 R259 S291 S292
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0015067 amidinotransferase activity
GO:0015068 glycine amidinotransferase activity
GO:0016740 transferase activity
Biological Process
GO:0006600 creatine metabolic process
GO:0006601 creatine biosynthetic process
GO:0007611 learning or memory
GO:0014889 muscle atrophy
GO:0120162 positive regulation of cold-induced thermogenesis
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005743 mitochondrial inner membrane
GO:0005758 mitochondrial intermembrane space
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1jdx, PDBe:1jdx, PDBj:1jdx
PDBsum1jdx
PubMed9915841
UniProtP50440|GATM_HUMAN Glycine amidinotransferase, mitochondrial (Gene Name=GATM)

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