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PDBsum entry 7vug

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protein ligands Protein-protein interface(s) links
Membrane protein PDB id
7vug

 

 

 

 

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Contents
Protein chains
218 a.a.
338 a.a.
57 a.a.
282 a.a.
232 a.a.
Ligands
7ZQ
PDB id:
7vug
Name: Membrane protein
Title: Cryo-em structure of a class a orphan gpcr in complex with gi
Structure: Guanine nucleotide-binding protein g(i) subunit alpha-1. Chain: a. Synonym: adenylate cyclase-inhibiting g alpha protein. Engineered: yes. Guanine nucleotide-binding protein g(i)/g(s)/g(t) subunit beta-1. Chain: b. Synonym: transducin beta chain 1. Engineered: yes.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gnai1. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Gene: gnb1. Gene: gng2. Bacillus circulans, homo sapiens.
Authors: Z.J.Liu,T.Hua,Y.L.Zhou,L.J.Wu
Key ref: Y.Zhou et al. Molecular insights into ligand recognition and g prot coupling of the neuromodulatory orphan receptor gpr13. Cell res, . PubMed id: 34916631
Date:
02-Nov-21     Release date:   29-Dec-21    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
P63096  (GNAI1_HUMAN) -  Guanine nucleotide-binding protein G(i) subunit alpha-1 from Homo sapiens
Seq:
Struc:
354 a.a.
218 a.a.
Protein chain
P62873  (GBB1_HUMAN) -  Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 from Homo sapiens
Seq:
Struc:
340 a.a.
338 a.a.
Protein chain
P59768  (GBG2_HUMAN) -  Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 from Homo sapiens
Seq:
Struc:
71 a.a.
57 a.a.
Protein chain
P09850  (XYNA_NIACI) -  Endo-1,4-beta-xylanase from Niallia circulans
Seq:
Struc:
213 a.a.
282 a.a.*
Protein chain
Q6DWJ6  (GP139_HUMAN) -  Probable G-protein coupled receptor 139 from Homo sapiens
Seq:
Struc:
353 a.a.
282 a.a.*
Protein chain
No UniProt id for this chain
Struc: 232 a.a.
Key:    Secondary structure
* PDB and UniProt seqs differ at 133 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class 2: Chain A: E.C.3.6.5.-  - ?????
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
   Enzyme class 3: Chain R: E.C.3.2.1.8  - endo-1,4-beta-xylanase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Endohydrolysis of 1,4-beta-D-xylosidic linkages in xylans.
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

 

 

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