Structure of PDB 2vxo Chain A

Receptor sequence
>2vxoA (length=643) Species: 9606 (Homo sapiens) [Search protein sequence]
EGAVVILDAGYGKVIDRRVRELFVQSEIFPLETPAFAIKEQGFRAIIISG
GPAPWFDPAIFTIGKPVLGICYGMQMMNKVFGGTVHKVFNISVDNTCSLF
RGLQKEEVVLLTHGDSVDKVADGFKVVARSGNIVAGIANESKKLYGAQFH
PEVGLTENGKVILKNFLYDIAGCSGTFTVQNRELECIREIKERVGTSKVL
VLLSGGVDSTVCTALLNRALNQEQVIAVHIDNGFMRKRESQSVEEALKKL
GIQVKVINAAHSFYNGTTTLPRISKTLNMTTSPEEKRKIIGDTFVKIANE
VIGEMNLKPEEVFLAQGTLRPDLIESASLVASGKAELIKTHHNDTELIRK
LREEGKVIEPLKDFHKDEVRILGRELGLPEELVSRHPFPGPGLAIRVICA
EEPYICKDFPETNNILKIVADFSASVKKPHTLLQRVKACTTEEDQEKLMQ
ITSLHSLNAFLLPIKTVGVQGDCRSYSYVCGISSKDEPDWESLIFLARLI
PRMCHNVNRVVYIFGPPVKEPPTDVTPTFLTTGVLSTLRQADFEAHNILR
ESGYAGKISQMPVILTPLHFDRDPLQKQPSCQRSVVIRTFITSDFMTGIP
ATPGNEIPVEVVLKMVTEIKKIPGISRIMYDLTSKPPGTTEWE
3D structure
PDB2vxo Substrate Specificity and Oligomerization of Human Gmp Synthetase
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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).
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 A R337 G383 K384 P439 G440 P441 Q610 F645 K685 T689 T690 E691 R287 G333 K334 P389 G390 P391 Q560 F595 K635 T639 T640 E641
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

View graph for
Molecular Function

View graph for
Biological Process

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

[Back to BioLiP]