Structure of PDB 2zj4 Chain A

Receptor sequence
>2zj4A (length=365) Species: 9606 (Homo sapiens) [Search protein sequence]
MKGNFSSFMQKEIFEQPESVVNTMRGRVNFDDYTVNLGGLKDHIKEIQRC
RRLILIACGTSYHAGVATRQVLEELTELPVMVELASDFLDRNTPVFRDDV
CFFLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINA
GPEIGVASTKAYTSQFVSLVMFALMMCDDRISMQERRKEIMLGLKRLPDL
IKEVLSMDDEIQKLATELYHQKSVLIMGRGYHYATCLEGALKIKEITYMH
SEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRP
VVICDKEDTETIKNTKRTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGY
DVDFPRNLAKSVTVE
3D structure
PDB2zj4 Structural analysis of human glutamine:fructose-6-phosphate amidotransferase, a key regulator in type 2 diabetes
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E553 K557 E560 H576 K675
Catalytic site (residue number reindexed from 1) E238 K242 E245 H261 K360
Enzyme Commision number 2.6.1.16: glutamine--fructose-6-phosphate transaminase (isomerizing).
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 AGP A T375 S376 S420 Q421 S422 T425 V471 A472 K557 E560 T60 S61 S105 Q106 S107 T110 V156 A157 K242 E245
Gene Ontology
Molecular Function
GO:0097367 carbohydrate derivative binding
Biological Process
GO:1901135 carbohydrate derivative metabolic process

View graph for
Molecular Function
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Biological Process
External links
PDB RCSB:2zj4, PDBe:2zj4, PDBj:2zj4
PDBsum2zj4
PubMed19059404
UniProtQ06210|GFPT1_HUMAN Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1 (Gene Name=GFPT1)

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