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3KA9

Frog M-ferritin, EEH mutant, with cobalt

Functional Information from GO Data
ChainGOidnamespacecontents
A0004322molecular_functionferroxidase activity
A0005737cellular_componentcytoplasm
A0006826biological_processiron ion transport
A0006879biological_processintracellular iron ion homeostasis
A0006880biological_processintracellular sequestering of iron ion
A0008198molecular_functionferrous iron binding
A0008199molecular_functionferric iron binding
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE CO A 176
ChainResidue
AHIS169
ACL187
ACL187
ACL187
AHIS169
AHIS169
AHIS169
ACL185
ACL185
ACL185
ACL185
ACL187

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 177
ChainResidue
AGLU23
AGLU58
AHIS61
AHOH376
AHOH381

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 178
ChainResidue
AGLU57
AGLU136
AHIS140
AHOH355
AHOH390

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 179
ChainResidue
AHIS56
AGLU60
AGLU63
AHOH449
AHOH450

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CO A 180
ChainResidue
AHOH323
AHOH323
AHOH323
AHOH378
AHOH378
AHOH378

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CO A 181
ChainResidue
AHOH302
AHOH302
AHOH302
AHOH405
AHOH405
AHOH405

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 182
ChainResidue
AHIS45
AGLU49
AHOH253
AHOH304
AHOH305

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 183
ChainResidue
ASER10
AHOH220
AHOH344
AHOH420
AHOH452
AHOH453

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 184
ChainResidue
AHOH284
AHOH418
AHOH448
AHOH454
AHOH456
AHOH475

site_idBC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE CL A 185
ChainResidue
ALEU165
ALEU165
ALEU165
ALEU165
AHIS169
AHIS169
AHIS169
AHIS169
ACO176
ACO176
ACO176
ACO176

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 186
ChainResidue
AASP87
AGLU88

site_idBC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CL A 187
ChainResidue
AHIS169
AHIS169
AHIS169
AHIS169
ACO176
ACO176
ACO176
ACO176

site_idBC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MG A 188
ChainResidue
AHOH235
AHOH235
AHOH345
AHOH345
AHOH385
AHOH385
AHOH393
AHOH393

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 189
ChainResidue
AASN46
AGLU49
AHOH233
AHOH293
AHOH307

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 190
ChainResidue
AHOH308
AHOH309
AHOH310
AHOH311
AHOH379
AHOH486

site_idBC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 191
ChainResidue
ATYR8
AARG5
AASN7

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 192
ChainResidue
ASER131
AGLU132
ATYR133
AGLU135
AGLU136

Functional Information from PROSITE/UniProt
site_idPS00204
Number of Residues21
DetailsFERRITIN_2 Ferritin iron-binding regions signature 2. DphLCDFLEseYLeeevkhIK
ChainResidueDetails
AASP122-LYS142

site_idPS00540
Number of Residues19
DetailsFERRITIN_1 Ferritin iron-binding regions signature 1. EeREhaEKFMkyQNkRgGR
ChainResidueDetails
AGLU57-ARG75

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING:
ChainResidueDetails
AGLU23
AGLU58
AHIS61
AGLU103
AGLU137
AHIS140

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PDB entries from 2024-07-24

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