Structure of PDB 5zlp Chain I

Receptor sequence
>5zlpI (length=475) Species: 85962 (Helicobacter pylori 26695) [Search protein sequence]
NSESKIKEFFEFCKENEVEFVDFRFSDIKGTWNHIAYSFGALTHGMLKEG
IPFDASCFKGWQGIEHSDMILTPDLVRYFIDPFSADVSVVVFCDVYDVYK
NQPYEKCPRSIAKKALQHLKDSGLGDVAYFGAENEFFIFDSIKIKDASNS
QYYEVDSEEGEWNRDRSFENGVNFGHRPGKQGGYMPVPPTDTMMDIRTEI
VKVLNQVGLETFVVHHEVAQAQGEVGVKFGDLVEAADNVQKLKYVVKMVA
HLNGKTATFMPKPLYGDNGSGMHTHVSVWKNNENLFSGETYKGLSEFALH
FLGGVLRHARGLAAFTNASTNSYKRLIPGYEAPSILTYSANNRSASVRIP
YGISKNSARFEFRFPDSSSNPYLAFAAILMAGMDGVKNKIDPGEAMDINL
FKLTLDEIREKGIKQMPHTLRRSLEEMLADKQYLKESQVFSEEFIQAYQS
LKFNAEVFPWESKPHPFEFITTYSC
3D structure
PDB5zlp Structural Analysis of Glutamine Synthetase from Helicobacter pylori.
ChainI
Resolution2.93 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 6.3.1.2: glutamine synthetase.
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 ADP I E139 F218 F235 H281 S283 R365 E133 F212 F229 H275 S277 R359
BS02 PPQ I E141 E223 N274 H279 R331 E337 R369 E135 E217 N268 H273 R325 E331 R363
BS03 MG I E141 E223 E230 E135 E217 E224
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004356 glutamine synthetase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0046872 metal ion binding
Biological Process
GO:0006542 glutamine biosynthetic process
GO:0019740 nitrogen utilization
Cellular Component
GO:0005737 cytoplasm
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5zlp, PDBe:5zlp, PDBj:5zlp
PDBsum5zlp
PubMed30076387
UniProtP94845|GLN1B_HELPY Glutamine synthetase (Gene Name=glnA)

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