Structure of PDB 6oy3 Chain B

Receptor sequence
>6oy3B (length=594) Species: 660122 (Fusarium vanettenii 77-13-4) [Search protein sequence]
SNFGVDFVIHYKVPAAERDEAEAGFVQLIRALTTVGLATEVRHGENESLL
VFVKVASPDLFAKQVYRARLGDWLHGVRVSAPIAQALQDEPVVEAERLRL
IYLMITKPHNWKHVESIFPLHSHSFNKEWIKKWSSKYTLEQTDIDNIRDK
FGESVAFYFAFLRSYFRFLVIPSAFGFGAWLLLGQFSYLYALLCGLWSVV
FFEYWKKQEVDLAVQWGVRGVSSIQQSRPEFEWEHEAVKVYPPMKRVKTQ
LLQIPFALACVVAAGALIVTCNSLEVFINEVGKQYLGFLPTIFLVIGTPT
ISGVLMGAAEKLNAMENYATVDAHDAALIQKQFVLNFMTSYMALFFTAFV
YIPFGHILHPFQINPARISNQMFYFTVTAQIVNFATEVVVPYIKQQAFQK
AKQDHEEEAEFLQRVREECTLEEYDVSGDYREMVMQFGYVAMFSVAWPLA
ACCFLVNNWVELRSDALKIAISSRRPIPWRTDSIGPWLTALSFLSWLGSI
TSSAIVYLCSASPLKAWGLLLSILFAEHFYLVVQLAVRFVLSKLDSPGLQ
KERKERFQTKKRLLQENLGWQRQRGMQETIEIGRRMIEQQLAAG
3D structure
PDB6oy3 Dynamic modulation of the lipid translocation groove generates a conductive ion channel in Ca 2+ -bound nhTMEM16.
ChainB
Resolution4.0 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 CA B N448 E506 E535 N383 E432 E461
BS02 CA B E452 E506 E535 E387 E432 E461
Gene Ontology
Molecular Function
GO:0005254 chloride channel activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
Biological Process
GO:1902476 chloride transmembrane transport
Cellular Component
GO:0016020 membrane
GO:0032541 cortical endoplasmic reticulum

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6oy3, PDBe:6oy3, PDBj:6oy3
PDBsum6oy3
PubMed31672969
UniProtC7Z7K1

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