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3UCW

Structure of MG2+ bound N-Terminal domain of Calmodulin

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
B0005509molecular_functioncalcium ion binding
C0005509molecular_functioncalcium ion binding
D0005509molecular_functioncalcium ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 100
ChainResidue
AASP20
AASP22
AASP24
ATHR26
AHOH208
AHOH224

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 101
ChainResidue
AHOH211
AHOH212
ATHR62
AHOH209
AHOH210

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 102
ChainResidue
AASP64
AHOH217
BASP64
BHOH201
BHOH202
BHOH212

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 100
ChainResidue
BASP20
BASP22
BASP24
BTHR26
BHOH204
BHOH205

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 101
ChainResidue
BTHR62
BHOH207
BHOH208
BHOH209
BHOH217

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG C 100
ChainResidue
CASP20
CASP22
CASP24
CTHR26
CHOH208
CHOH209

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG C 101
ChainResidue
CTHR62
CHOH204
CHOH205
CHOH206
CHOH216

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG C 102
ChainResidue
CASP64
CHOH202
CHOH203
CHOH219
CHOH220
DASP64

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG D 100
ChainResidue
DASP20
DASP22
DASP24
DTHR26
DHOH201
DHOH202

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG D 101
ChainResidue
DTHR62
DHOH203
DHOH204
DHOH212
DHOH230

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
ChainResidueDetails
AASP20-LEU32
AASP56-PHE68

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03
ChainResidueDetails
AASP20
AGLU67
BASP20
BASP22
BASP24
BTHR26
BGLU31
BASP56
BASP58
BASN60
BTHR62
AASP22
BGLU67
CASP20
CASP22
CASP24
CTHR26
CGLU31
CASP56
CASP58
CASN60
CTHR62
AASP24
CGLU67
DASP20
DASP22
DASP24
DTHR26
DGLU31
DASP56
DASP58
DASN60
DTHR62
ATHR26
DGLU67
AGLU31
AASP56
AASP58
AASN60
ATHR62

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:7093203, ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712
ChainResidueDetails
AALA1
BALA1
CALA1
DALA1

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS21
BLYS21
CLYS21
DLYS21

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphothreonine; by CaMK4 => ECO:0000250|UniProtKB:P0DP29
ChainResidueDetails
ATHR44
BTHR44
CTHR44
DTHR44

site_idSWS_FT_FI5
Number of Residues8
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62157
ChainResidueDetails
ALYS21
BLYS21
CLYS21
DLYS21

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PDB entries from 2024-09-11

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