Structure of PDB 2vxo Chain A Binding Site BS01

Receptor Information
>2vxo Chain A (length=643) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EGAVVILDAGYGKVIDRRVRELFVQSEIFPLETPAFAIKEQGFRAIIISG
GPAPWFDPAIFTIGKPVLGICYGMQMMNKVFGGTVHKVFNISVDNTCSLF
RGLQKEEVVLLTHGDSVDKVADGFKVVARSGNIVAGIANESKKLYGAQFH
PEVGLTENGKVILKNFLYDIAGCSGTFTVQNRELECIREIKERVGTSKVL
VLLSGGVDSTVCTALLNRALNQEQVIAVHIDNGFMRKRESQSVEEALKKL
GIQVKVINAAHSFYNGTTTLPRISKTLNMTTSPEEKRKIIGDTFVKIANE
VIGEMNLKPEEVFLAQGTLRPDLIESASLVASGKAELIKTHHNDTELIRK
LREEGKVIEPLKDFHKDEVRILGRELGLPEELVSRHPFPGPGLAIRVICA
EEPYICKDFPETNNILKIVADFSASVKKPHTLLQRVKACTTEEDQEKLMQ
ITSLHSLNAFLLPIKTVGVQGDCRSYSYVCGISSKDEPDWESLIFLARLI
PRMCHNVNRVVYIFGPPVKEPPTDVTPTFLTTGVLSTLRQADFEAHNILR
ESGYAGKISQMPVILTPLHFDRDPLQKQPSCQRSVVIRTFITSDFMTGIP
ATPGNEIPVEVVLKMVTEIKKIPGISRIMYDLTSKPPGTTEWE
Ligand information
Ligand IDXMP
InChIInChI=1S/C10H13N4O9P/c15-5-3(1-22-24(19,20)21)23-9(6(5)16)14-2-11-4-7(14)12-10(18)13-8(4)17/h2-3,5-6,9,15-16H,1H2,(H2,19,20,21)(H2,12,13,17,18)/p+1/t3-,5-,6-,9-/m1/s1
InChIKeyDCTLYFZHFGENCW-UUOKFMHZSA-O
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1[nH+]c2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)COP(=O)(O)O)O)O)NC(=O)NC2=O
CACTVS 3.341O[C@H]1[C@@H](O)[C@@H](O[C@@H]1CO[P](O)(O)=O)n2c[nH+]c3C(=O)NC(=O)Nc23
OpenEye OEToolkits 1.5.0c1[nH+]c2c(n1C3C(C(C(O3)COP(=O)(O)O)O)O)NC(=O)NC2=O
ACDLabs 10.04O=C3Nc1c([nH+]cn1C2OC(C(O)C2O)COP(=O)(O)O)C(=O)N3
CACTVS 3.341O[CH]1[CH](O)[CH](O[CH]1CO[P](O)(O)=O)n2c[nH+]c3C(=O)NC(=O)Nc23
FormulaC10 H14 N4 O9 P
NameXANTHOSINE-5'-MONOPHOSPHATE;
5-MONOPHOSPHATE-9-BETA-D-RIBOFURANOSYL XANTHINE
ChEMBL
DrugBank
ZINC
PDB chain2vxo Chain A Residue 1694 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB2vxo Substrate Specificity and Oligomerization of Human Gmp Synthetase
Resolution2.5 Å
Binding residue
(original residue number in PDB)		R337 G383 K384 P439 G440 P441 Q610 F645 K685 T689 T690 E691
Binding residue
(residue number reindexed from 1)		R287 G333 K334 P389 G390 P391 Q560 F595 K635 T639 T640 E641
Annotation score2
Enzymatic activity
Catalytic site (original residue number in PDB) G77 C104 Y105 H190 E192 D248 K416
Catalytic site (residue number reindexed from 1) G51 C71 Y72 H150 E152 D208 K366
Enzyme Commision number 6.3.5.2: GMP synthase (glutamine-hydrolyzing).
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:0009113 purine nucleobase biosynthetic process
GO:0009168 purine ribonucleoside monophosphate biosynthetic process
GO:0046037 GMP metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2vxo, PDBe:2vxo, PDBj:2vxo
PDBsum2vxo
PubMed23816837
UniProtP49915|GUAA_HUMAN GMP synthase [glutamine-hydrolyzing] (Gene Name=GMPS)

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