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6IIH

crystal structure of mitochondrial calcium uptake 2(MICU2)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0003824molecular_functioncatalytic activity
A0005509molecular_functioncalcium ion binding
A0006851biological_processmitochondrial calcium ion transmembrane transport
A0008152biological_processmetabolic process
A0009253biological_processpeptidoglycan catabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016998biological_processcell wall macromolecule catabolic process
A0030430cellular_componenthost cell cytoplasm
A0031640biological_processkilling of cells of another organism
A0042742biological_processdefense response to bacterium
A0044659biological_processviral release from host cell by cytolysis
B0003796molecular_functionlysozyme activity
B0003824molecular_functioncatalytic activity
B0005509molecular_functioncalcium ion binding
B0006851biological_processmitochondrial calcium ion transmembrane transport
B0008152biological_processmetabolic process
B0009253biological_processpeptidoglycan catabolic process
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0016998biological_processcell wall macromolecule catabolic process
B0030430cellular_componenthost cell cytoplasm
B0031640biological_processkilling of cells of another organism
B0042742biological_processdefense response to bacterium
B0044659biological_processviral release from host cell by cytolysis
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CA A 501
ChainResidue
AASP264
AASP266
AASN268
AMET270
AGLU275
AHOH630

site_idAC2
Number of Residues6
Detailsbinding site for residue CA B 501
ChainResidue
BMET270
BGLU272
BGLU275
BASP264
BASP266
BASN268

site_idAC3
Number of Residues6
Detailsbinding site for residue CA B 502
ChainResidue
BASP454
BASP456
BASP458
BCYS460
BGLU465
BHOH728

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
ChainResidueDetails
AGLU11
BGLU11

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
ChainResidueDetails
AASP20
BASP20

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:8266098
ChainResidueDetails
BLEU32
BPHE104
ALEU32
APHE104

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000303|PubMed:7831309
ChainResidueDetails
ASER117
AASN132
BSER117
BASN132

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ASER284
BSER284

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
AGLU11proton shuttle (general acid/base)
AASP20covalent catalysis

site_idMCSA2
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
BGLU11proton shuttle (general acid/base)
BASP20covalent catalysis

218500

PDB entries from 2024-04-17

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