Structure of PDB 5tw7 Chain E

Receptor sequence
>5tw7E (length=489) Species: 485 (Neisseria gonorrhoeae) [Search protein sequence]
QDKILILDFGSQVTRLIARRVREAHVYCELHSFDMPLDEIKAFNPKGIIL
SGGPNSVYESDYQADTGIFDLGIPVLGICYGMQFMAHHLGGEVQPGNQRE
FGYAQVKTIDSGLTRGIQDDAPNTLDVWMSHGDKVSKLPDGFAVIGDTPS
CPIAMMENTEKQFYGIQFHPEVTHTKQGRALLNRFVLDICGAQPGWTMPN
YIEEAVAKIREQVGSDEVILGLSGGVDSSVAAALIHRAIGDQLTCVFVDH
GLLRLNEGKMVMDMFARNLGVKVIHVDAEGQFMAKLAGVTDPEKKRKIIG
AEFIEVFDAEEKKLTNAKWLAQGTIYPDVILKLLEPLRDLFKDEVRELGV
ALGLPREMVYRHPFPGPGLGVRILGEVKKEYADLLRQADDIFIQELRNTT
DENGTSWYDLTSQAFAVFLPVKSVGVMRTYDYVVALRAVITSDFMTAHWA
ELPYSLLGRVSNRIINEVKGINRVVYDVSGKPPATIEWE
3D structure
PDB5tw7 Crystal structure of a GMP synthase (glutamine-hydrolyzing) from Neisseria gonorrhoeae
ChainE
Resolution2.35 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G55 C81 Y82 H171 E173 D229 K371
Catalytic site (residue number reindexed from 1) G53 C79 Y80 H169 E171 D227 K342
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 MG E I497 V500 I503 I465 V468 I471
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:0046037 GMP metabolic process
Cellular Component
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:5tw7, PDBe:5tw7, PDBj:5tw7
PDBsum5tw7
PubMed
UniProtB4RJH7|GUAA_NEIG2 GMP synthase [glutamine-hydrolyzing] (Gene Name=guaA)

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