Structure of PDB 7cqq Chain B Binding Site BS04

Receptor Information
>7cqq Chain B (length=429) Species: 2203891 (Rhodovulum sp. 12E13) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TDLASIAREKGIEFFLISFTDLLGVQRAKLVPARAIADMAVNGAGFAGFA
AWLDMSPADADILAIPDPESLIQLPWKPSVGWLAADVHFEGRPFPKAPRV
ALKSVLARAAGKDMHLKHGVECEFFLIQPDGSAISDPADTQAKPCYDQDA
LMRRFDVIAEICSYMVDLGWGPYQNDHEDANGQFEMNWDYADALVTADRH
AFFKFMVKSVAERHGLRATFMPKPFAHLTGNGCHTHLSMWTAAGDNLFEG
DGELGLSPTAYAFLGGLIGHAKGLTAVVNPTVNSYKRLNAPVTVSGATWS
PNTITYGGNNRTHMVRIPDAGRLELRLPDGAANPYLMPAAILAAGLDGIE
TQADPGQRLDIDMYVEGHSVEAEQLPLNLLDAVRALEADEVLAGGLGAAA
AAFAKFKRAEWADYKSQLTEWERRTTLDC
Ligand information
Ligand IDANP
InChIInChI=1S/C10H17N6O12P3/c11-8-5-9(13-2-12-8)16(3-14-5)10-7(18)6(17)4(27-10)1-26-31(24,25)28-30(22,23)15-29(19,20)21/h2-4,6-7,10,17-18H,1H2,(H,24,25)(H2,11,12,13)(H4,15,19,20,21,22,23)/t4-,6-,7-,10-/m1/s1
InChIKeyPVKSNHVPLWYQGJ-KQYNXXCUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(NP(=O)(O)O)O)O)O)N
CACTVS 3.370Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)N[P](O)(O)=O)[CH](O)[CH]3O
CACTVS 3.370Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P](O)(=O)O[P](O)(=O)N[P](O)(O)=O)[C@@H](O)[C@H]3O
ACDLabs 12.01O=P(O)(O)NP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
OpenEye OEToolkits 1.7.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)O[P@@](=O)(NP(=O)(O)O)O)O)O)N
FormulaC10 H17 N6 O12 P3
NamePHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
ChEMBLCHEMBL1230989
DrugBank
ZINCZINC000008660410
PDB chain7cqq Chain B Residue 504 [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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PDB7cqq Crystal structures of gamma-glutamylmethylamide synthetase provide insight into bacterial metabolism of oceanic monomethylamine.
Resolution2.295 Å
Binding residue
(original residue number in PDB)		E122 Y174 E186 N188 W189 Y191 H235 H237 S239 R312 R317 R323 E325
Binding residue
(residue number reindexed from 1)		E121 Y173 E185 N187 W188 Y190 H234 H236 S238 R311 R316 R322 E324
Annotation score3
Enzymatic activity
Enzyme Commision number 6.3.1.2: glutamine synthetase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003824 catalytic activity
GO:0004356 glutamine synthetase activity
GO:0016874 ligase activity
GO:0046872 metal ion binding
Biological Process
GO:0006542 glutamine biosynthetic process
GO:0009399 nitrogen fixation

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:7cqq, PDBe:7cqq, PDBj:7cqq
PDBsum7cqq
PubMed33199371
UniProtA0A369R1N0

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