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5TSA

Crystal structure of the Zrt-/Irt-like protein from Bordetella bronchiseptica with bound Zn2+

Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0006829biological_processzinc ion transport
A0016020cellular_componentmembrane
A0030001biological_processmetal ion transport
A0046873molecular_functionmetal ion transmembrane transporter activity
A0055085biological_processtransmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue ZN A 401
ChainResidue
AGLU181
AGLN207
AGLU211
AHOH503
AHOH504

site_idAC2
Number of Residues5
Detailsbinding site for residue ZN A 402
ChainResidue
AHOH511
ALEU224
AHOH506
AHOH509
AHOH510

site_idAC3
Number of Residues2
Detailsbinding site for residue ZN A 403
ChainResidue
AHIS177
AGLU276

site_idAC4
Number of Residues2
Detailsbinding site for residue ZN A 404
ChainResidue
AASP144
AHIS275

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN A 405
ChainResidue
AASP144
AHIS177
AHOH505
AHOH508

site_idAC6
Number of Residues2
Detailsbinding site for residue ZN A 406
ChainResidue
AASP89
AHIS286

site_idAC7
Number of Residues6
Detailsbinding site for residue CD A 407
ChainResidue
AASN178
AGLU181
AASP208
AGLU211
AGLU240
AHOH507

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues21
DetailsTOPO_DOM: Periplasmic => ECO:0000269|PubMed:35857505
ChainResidueDetails
AMET1-HIS22

site_idSWS_FT_FI2
Number of Residues27
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:35857505
ChainResidueDetails
APRO23-GLY50

site_idSWS_FT_FI3
Number of Residues4
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:35857505
ChainResidueDetails
AGLU51-HIS55

site_idSWS_FT_FI4
Number of Residues201
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:28875161
ChainResidueDetails
AVAL56-ARG81
ASER84-VAL119
AGLY122-TYR145
AARG166-ALA190
AASP193-VAL222
APRO225-SER251
ALEU256-HIS275
ATHR288-LEU308

site_idSWS_FT_FI5
Number of Residues32
DetailsTOPO_DOM: Periplasmic => ECO:0000305|PubMed:28875161
ChainResidueDetails
AALA82-ILE83
APHE146-ASN165
AGLY223-LEU224
AGLU276-GLU287

site_idSWS_FT_FI6
Number of Residues6
DetailsTOPO_DOM: Extracellular => ECO:0000305|PubMed:28875161
ChainResidueDetails
AGLY120-PRO121
ATHR191-GLY192
ASER252-ALA255
AGLY309

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: M7 metal binding site => ECO:0000269|PubMed:28875161, ECO:0007744|PDB:5TSA
ChainResidueDetails
AASP89
AHIS286

site_idSWS_FT_FI8
Number of Residues1
DetailsBINDING: M1 metal binding site => ECO:0000269|PubMed:28875161, ECO:0000269|PubMed:31914589, ECO:0000269|PubMed:35857505, ECO:0007744|PDB:5TSB, ECO:0007744|PDB:6PGI, ECO:0007744|PDB:7Z6M
ChainResidueDetails
AMET99

site_idSWS_FT_FI9
Number of Residues1
DetailsBINDING: M6 metal binding site => ECO:0000269|PubMed:28875161, ECO:0007744|PDB:5TSA
ChainResidueDetails
AASP144

site_idSWS_FT_FI10
Number of Residues2
DetailsBINDING: M5 metal binding site => ECO:0000269|PubMed:28875161, ECO:0007744|PDB:5TSA
ChainResidueDetails
AHIS177
AGLU276

site_idSWS_FT_FI11
Number of Residues3
DetailsBINDING: M2 metal binding site => ECO:0000269|PubMed:28875161, ECO:0007744|PDB:5TSA, ECO:0007744|PDB:5TSB
ChainResidueDetails
AASN178
AASP208
AGLU240

site_idSWS_FT_FI12
Number of Residues3
DetailsBINDING: M1 metal binding site => ECO:0000269|PubMed:28875161, ECO:0007744|PDB:5TSA
ChainResidueDetails
AGLU181
AGLN207
AGLU211

site_idSWS_FT_FI13
Number of Residues1
DetailsBINDING: M3 metal binding site => ECO:0000269|PubMed:28875161, ECO:0007744|PDB:5TSA
ChainResidueDetails
AHIS275

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PDB entries from 2024-07-24

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