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4QNH

Calcium-calmodulin (T79D) complexed with the calmodulin binding domain from a small conductance potassium channel SK2-a

Functional Information from GO Data
ChainGOidnamespacecontents
B0005516molecular_functioncalmodulin binding
B0006813biological_processpotassium ion transport
B0015269molecular_functioncalcium-activated potassium channel activity
B0016020cellular_componentmembrane
B0016286molecular_functionsmall conductance calcium-activated potassium channel activity
R0005509molecular_functioncalcium ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 501
ChainResidue
BLYS451
BHIS452
BHOH639
BHOH640
BHOH663

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA R 1001
ChainResidue
RGLU31
RHOH1103
RASP20
RASP22
RASP24
RTHR26

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA R 1002
ChainResidue
RASP56
RASP58
RASN60
RTHR62
RGLU67
RHOH1219

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
ChainResidueDetails
RASP20-LEU32
RASP56-PHE68
RASP93-LEU105
RASP129-PHE141

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
ChainResidueDetails
RASP20
RGLU67
RASP93
RASP95
RASN97
RTYR99
RGLU104
RASP129
RASP131
RASP133
RGLN135
RASP22
RGLU140
RASP24
RTHR26
RGLU31
RASP56
RASP58
RASN60
RTHR62

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:201628, ECO:0000269|Ref.9
ChainResidueDetails
RALA1

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P0DP25
ChainResidueDetails
RLYS21

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by CaMK4 => ECO:0000269|PubMed:12392717
ChainResidueDetails
RTHR44

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P0DP25
ChainResidueDetails
RSER81

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P0DP25
ChainResidueDetails
RLYS94

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:22673903
ChainResidueDetails
RTYR99

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
RSER101

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P0DP25
ChainResidueDetails
RTHR110

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:P0DP25
ChainResidueDetails
RLYS115

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P0DP25
ChainResidueDetails
RTYR138

site_idSWS_FT_FI12
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62157
ChainResidueDetails
RLYS21

221716

PDB entries from 2024-06-26

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