Structure of PDB 2ywc Chain C

Receptor sequence

>2ywcC (length=467) Species: 300852 (Thermus thermophilus HB8)

MVLVLDFGSQYTRLIARRLRELRAFSLILPGDAPLEEVLKHRPQALILSG
GPRSVFDPDAPRPDPRLFSSGLPLLGICYGMQLLAQELGGRVERAGRAEY
GKALLTRHEGPLFRGLEGEVQVWMSHQDAVTAPPPGWRVVAETEENPVAA
IASPDGRAYGVQFHPEVAHTPKGMQILENFLELAGVKRDWTPEHVLEELL
REVRERAGKDRVLLAVSGGVDSSTLALLLAKAGVDHLAVFVDHGLLRLGE
REEVEGALRALGVNLLVVDAKERFLKALKGVEDPEEKRKIIGREFVAAFS
QVARERGPFRFLAQGTLYPDVIEFELLEPFRLLFKDEVRELALLLGLPDT
LRLRHPFPGPGLAVRVLGEVTEERLEILRRADDIFTSLLREWGLYEKVAQ
ALAVLTPVGYVLALRAVTTEDFMTADWARLPLEFLDEAARRITRRVPEIG
RVVYDLTSKPPATIEWE

3D structure

• PDB: 2ywc Crystal structure of GMP synthetase from Thermus thermophilus
• Chain: C
• Resolution: 2.2 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): G51 R53 C78 Y79 H164 E166 D221 K359
• Catalytic site (residue number reindexed from 1): G51 R53 C78 Y79 H164 E166 D221 K335
• Enzyme Commision number: 6.3.5.2: GMP synthase (glutamine-hydrolyzing).

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	XMP	C	R288 P382 G383 P384 Q424 F458 K495 T499 I500 E501	R288 P358 G359 P360 Q400 F422 K459 T463 I464 E465

Gene Ontology

Molecular Function

• GO:0003921 GMP synthase activity
• GO:0003922 GMP synthase (glutamine-hydrolyzing) activity
• GO:0005524 ATP binding
• GO:0016874 ligase activity

Biological Process

• GO:0006164 purine nucleotide biosynthetic process
• GO:0006177 GMP biosynthetic process
• GO:0006541 glutamine metabolic process
• GO:0044281 small molecule metabolic process

Cellular Component

• GO:0005829 cytosol

External links

• PDB: RCSB:2ywc, PDBe:2ywc, PDBj:2ywc
• PDBsum: 2ywc
• UniProt: Q5SI28|GUAA_THET8 GMP synthase [glutamine-hydrolyzing] (Gene Name=guaA)