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3U6N

Open Structure of the BK channel Gating Ring

Functional Information from GO Data
ChainGOidnamespacecontents
A0006813biological_processpotassium ion transport
A0016020cellular_componentmembrane
B0006813biological_processpotassium ion transport
B0016020cellular_componentmembrane
C0006813biological_processpotassium ion transport
C0016020cellular_componentmembrane
D0006813biological_processpotassium ion transport
D0016020cellular_componentmembrane
E0006813biological_processpotassium ion transport
E0016020cellular_componentmembrane
F0006813biological_processpotassium ion transport
F0016020cellular_componentmembrane
G0006813biological_processpotassium ion transport
G0016020cellular_componentmembrane
H0006813biological_processpotassium ion transport
H0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 2001
ChainResidue
AGLN893
AASP896
AGLN897
AASP899
AASP901
HASN449

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 2001
ChainResidue
BASP899
BASP901
GASN449
BGLN893
BASP896
BGLN897

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 2001
ChainResidue
CGLN893
CASP896
CGLN897
CASP899
CASP901
FASN449

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA D 2001
ChainResidue
CASN449
DGLN893
DASP896
DGLN897
DASP899
DASP901

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA E 2001
ChainResidue
DASN449
EGLN893
EASP896
EGLN897
EASP899
EASP901

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA F 2001
ChainResidue
EASN449
FGLN893
FASP896
FGLN897
FASP899
FASP901

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA G 2001
ChainResidue
AASN449
GGLN893
GASP896
GGLN897
GASP899
GASP901

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA H 2001
ChainResidue
BASN449
HGLN893
HASP896
HGLN897
HASP899
HASP901

Functional Information from PROSITE/UniProt
site_idPS00092
Number of Residues7
DetailsN6_MTASE N-6 Adenine-specific DNA methylases signature. VITNPPY
ChainResidueDetails
AVAL1037-TYR1043

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AGLU374
DGLU374
DGLN397
DGLU399
EGLU374
EGLN397
EGLU399
FGLU374
FGLN397
FGLU399
GGLU374
AGLN397
GGLN397
GGLU399
HGLU374
HGLN397
HGLU399
AGLU399
BGLU374
BGLN397
BGLU399
CGLU374
CGLN397
CGLU399

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0007744|PDB:3U6N
ChainResidueDetails
AASN449
BASN449
CASN449
DASN449
EASN449
FASN449
GASN449
HASN449

site_idSWS_FT_FI3
Number of Residues32
DetailsBINDING: BINDING => ECO:0000269|PubMed:22139424, ECO:0007744|PDB:3U6N
ChainResidueDetails
ALEU927
CALA930
CPHE933
CASP935
DLEU927
DALA930
DPHE933
DASP935
ELEU927
EALA930
EPHE933
AALA930
EASP935
FLEU927
FALA930
FPHE933
FASP935
GLEU927
GALA930
GPHE933
GASP935
HLEU927
APHE933
HALA930
HPHE933
HASP935
AASP935
BLEU927
BALA930
BPHE933
BASP935
CLEU927

site_idSWS_FT_FI4
Number of Residues16
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q08460
ChainResidueDetails
ATHR644
EGLU885
FTHR644
FGLU885
GTHR644
GGLU885
HTHR644
HGLU885
AGLU885
BTHR644
BGLU885
CTHR644
CGLU885
DTHR644
DGLU885
ETHR644

site_idSWS_FT_FI5
Number of Residues40
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q08460
ChainResidueDetails
ASER646
BGLN897
CSER646
CSER659
CSER663
CGLN893
CGLN897
DSER646
DSER659
DSER663
DGLN893
ASER659
DGLN897
ESER646
ESER659
ESER663
EGLN893
EGLN897
FSER646
FSER659
FSER663
FGLN893
ASER663
FGLN897
GSER646
GSER659
GSER663
GGLN893
GGLN897
HSER646
HSER659
HSER663
HGLN893
AGLN893
HGLN897
AGLN897
BSER646
BSER659
BSER663
BGLN893

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PDB entries from 2024-09-11

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