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3R2H

1.7 A resolution structure of As-Isolated FtnA from Pseudomonas aeruginosa (pH 10.5)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004322molecular_functionferroxidase activity
A0005506molecular_functioniron ion binding
A0005829cellular_componentcytosol
A0006826biological_processiron ion transport
A0006879biological_processintracellular iron ion homeostasis
A0006880biological_processintracellular sequestering of iron ion
A0008199molecular_functionferric iron binding
A0016491molecular_functionoxidoreductase activity
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CXS A 155
ChainResidue
AARG70
AASP74
AHIS77
ALYS91
AHIS95
AHOH191
AHOH193
AHOH264
AHOH300

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 156
ChainResidue
AGLU18
AGLU51
AHIS54
ANA157
AHOH304
AHOH307

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 157
ChainResidue
AGLU51
AGLU93
ANA156
AHOH281
AHOH303
AHOH307

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NA A 158
ChainResidue
AASN148
AASN148
AASN148
AASN148
AGLN151
AGLN151
AGLN151
AGLN151

Functional Information from PROSITE/UniProt
site_idPS00549
Number of Residues19
DetailsBACTERIOFERRITIN Bacterioferritin signature. MqGhpeVIdyLntlLtgeL
ChainResidueDetails
AMET1-LEU19

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00085
ChainResidueDetails
AGLU18
AGLU51
AHIS54
AGLU93
AGLU127
AHIS130

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00085
ChainResidueDetails
AMET48

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PDB entries from 2024-07-24

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