Structure of PDB 2qzy Chain A

Receptor sequence

>2qzyA (length=596) Species: 9031 (Gallus gallus)

LSTSLSALPAAARDFVEEAVRLCRPREVLLCDGSEEEGKELLRGLQDDGV
LHPLPKYDNCWLARTDPRDVARVESKTVLVTPEQSDAVPPPPPSGGPPQL
GNWMSPNAFQAAVQERFPGCMAGRPLYVIPFSMGPPTSPLAKLGVQVTDS
PYVVLSMRIMTRVGPAVLQRLDDDFVRCLHSVGRPLPLTEPLVSSWPCDP
SRVLVAHIPSERRIVSFGSGYGGNSLLGKKCFALRIASRMAQQQGWLAEH
MLILGVTSPSGEKRYMAAAFPSACGKTNLAMMTPSLPGWRIHCVGDDIAW
MKFDDEGRLRAINPERGFFGVAPGTSSRTNPNAMATIARNTIFTNVGLRS
DGGVYWDGLDEPTEPGVTYTSWLGKPWKHGDPEPCAHPNSRFCAPADQCP
IMDPRWDDPEGVPIDAIIFGGRRPRGVPLVVEAFGWRHGVFMGSAMRSLM
HDPFAMRPFFGYNAGRYLEHWLSTGLRSNARLPRLFHVNWFLRDNEGRFV
WPGFGHNARVLAWIFGRIQGRDTARPTPIGWVPKEGDLDLGGLPGVDYSQ
LFPMEKGFWEEECRQLREYYGENFGADLPRDVMAELEGLEERVRKM

3D structure

• PDB: 2qzy Structural Insights into the Mechanism of PEPCK Catalysis
• Chain: A
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R105 Y254 K263 H283 S305 C307 D330 R424
• Catalytic site (residue number reindexed from 1): R72 Y221 K230 H250 S272 C274 D297 R391
• Enzyme Commision number: 4.1.1.32: phosphoenolpyruvate carboxykinase (GTP).

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	TQY	A	F467 W576	F434 W531
BS02	FRU	A	F467 R470 E630 R637	F434 R437 E585 R592
BS03	MN	A	K263 H283 D330	K230 H250 D297
BS04	PEP	A	R105 Y254 G256 R424	R72 Y221 G223 R391

Gene Ontology

Molecular Function

• GO:0004611 phosphoenolpyruvate carboxykinase activity
• GO:0004613 phosphoenolpyruvate carboxykinase (GTP) activity
• GO:0005525 GTP binding
• GO:0017076 purine nucleotide binding

Biological Process

• GO:0006094 gluconeogenesis

External links

• PDB: RCSB:2qzy, PDBe:2qzy, PDBj:2qzy
• PDBsum: 2qzy
• PubMed: 16819824
• UniProt: P21642|PCKGM_CHICK Phosphoenolpyruvate carboxykinase [GTP], mitochondrial (Gene Name=PCK2)