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5LZR

Crystal structure of Thermotoga maritima sodium pumping membrane integral pyrophosphatase in complex with tungstate and magnesium

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004427molecular_functioninorganic diphosphate phosphatase activity
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0006814biological_processsodium ion transport
A0009678molecular_functiondiphosphate hydrolysis-driven proton transmembrane transporter activity
A0015081molecular_functionsodium ion transmembrane transporter activity
A0016020cellular_componentmembrane
A0030955molecular_functionpotassium ion binding
A0035725biological_processsodium ion transmembrane transport
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
A1902600biological_processproton transmembrane transport
B0000287molecular_functionmagnesium ion binding
B0004427molecular_functioninorganic diphosphate phosphatase activity
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005886cellular_componentplasma membrane
B0006814biological_processsodium ion transport
B0009678molecular_functiondiphosphate hydrolysis-driven proton transmembrane transporter activity
B0015081molecular_functionsodium ion transmembrane transporter activity
B0016020cellular_componentmembrane
B0030955molecular_functionpotassium ion binding
B0035725biological_processsodium ion transmembrane transport
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
B1902600biological_processproton transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue WO4 A 801
ChainResidue
ALYS664
AMG802
AMG803

site_idAC2
Number of Residues4
Detailsbinding site for residue MG A 802
ChainResidue
AASP660
AASP692
AWO4801
AMG803

site_idAC3
Number of Residues4
Detailsbinding site for residue MG A 803
ChainResidue
AWO4801
AMG802
AASP202
AASP232

site_idAC4
Number of Residues3
Detailsbinding site for residue WO4 B 801
ChainResidue
BASP465
BMG802
BMG803

site_idAC5
Number of Residues3
Detailsbinding site for residue MG B 802
ChainResidue
BASP465
BASN492
BWO4801

site_idAC6
Number of Residues3
Detailsbinding site for residue MG B 803
ChainResidue
BASP688
BASP692
BWO4801

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues800
DetailsTRANSMEM: Helical
ChainResidueDetails
ATYR2-PHE22
AILE406-PHE430
ALEU437-ILE463
ATHR493-SER520
AALA542-MET571
AILE602-LEU629
AALA631-ALA658
AVAL698-HIS722
BTYR2-PHE22
BASP47-PHE71
BTRP74-MET97
AASP47-PHE71
BTYR123-GLY153
BPHE169-TYR197
BASP236-TYR261
BALA285-ILE309
BLEU321-TYR343
BALA359-TRP379
BILE406-PHE430
BLEU437-ILE463
BTHR493-SER520
BALA542-MET571
ATRP74-MET97
BILE602-LEU629
BALA631-ALA658
BVAL698-HIS722
ATYR123-GLY153
APHE169-TYR197
AASP236-TYR261
AALA285-ILE309
ALEU321-TYR343
AALA359-TRP379

site_idSWS_FT_FI2
Number of Residues428
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:22837527
ChainResidueDetails
AALA23-ALA46
BALA98-ALA122
BTHR198-GLY235
BVAL310-GLU320
BALA380-VAL405
BALA464-ASN492
BLYS572-GLU601
BTRP659-THR697
AALA98-ALA122
ATHR198-GLY235
AVAL310-GLU320
AALA380-VAL405
AALA464-ASN492
ALYS572-GLU601
ATRP659-THR697
BALA23-ALA46

site_idSWS_FT_FI3
Number of Residues160
DetailsTOPO_DOM: Periplasmic => ECO:0000269|PubMed:22837527
ChainResidueDetails
ATHR72-THR73
BGLN154-ASN168
BMET262-GLN284
BLEU344-GLY358
BALA431-GLY436
BGLN521-ASP541
BGLY630
BVAL723-PHE726
AGLN154-ASN168
AMET262-GLN284
ALEU344-GLY358
AALA431-GLY436
AGLN521-ASP541
AGLY630
AVAL723-PHE726
BTHR72-THR73

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING:
ChainResidueDetails
ALYS199
ALYS695
BLYS199
BLYS695

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASP202
AASP206
BASP202
BASP206

site_idSWS_FT_FI6
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:22837527
ChainResidueDetails
AASN229
AASP232
AASP465
BASN229
BASP232
BASP465

site_idSWS_FT_FI7
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:22837527, ECO:0007744|PDB:4AV3
ChainResidueDetails
AASP660
AASP688
AASP692
BASP660
BASP688
BASP692

site_idSWS_FT_FI8
Number of Residues10
DetailsSITE: Important for ion transport => ECO:0000250
ChainResidueDetails
AARG191
BLYS707
AASP236
AASP243
AASP696
ALYS707
BARG191
BASP236
BASP243
BASP696

site_idSWS_FT_FI9
Number of Residues2
DetailsSITE: Determinant of potassium dependence => ECO:0000255|HAMAP-Rule:MF_01129, ECO:0000305
ChainResidueDetails
AALA495
BALA495

220113

PDB entries from 2024-05-22

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