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3KA6

Frog M-ferritin, EED mutant, with cobalt

Functional Information from GO Data
ChainGOidnamespacecontents
A0004322molecular_functionferroxidase activity
A0005737cellular_componentcytoplasm
A0006826biological_processiron ion transport
A0006879biological_processintracellular iron ion homeostasis
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
AHOH430
AHOH430
AHOH430
AHIS169
AHIS169
AHIS169
ACL189
ACL189
ACL189
ACL189
AHOH430

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CO A 177
ChainResidue
AGLU23
AGLU58
AHIS61
ACO178
AHOH386
AHOH387

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CO A 178
ChainResidue
AHIS54
AGLU58
AGLU103
ACO177
ACO184
AHOH347
AHOH387
AHOH491

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 179
ChainResidue
AHIS56
AGLU60
AGLU63
AHOH469
AHOH489

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CO A 180
ChainResidue
AHOH352
AHOH352
AHOH352
AHOH411
AHOH411
AHOH411

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CO A 181
ChainResidue
AASP41
AHOH238
AHOH252
AHOH264
AHOH332
AHOH433

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 182
ChainResidue
AHIS45
AGLU49
AHOH259
AHOH336
AHOH337

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CO A 183
ChainResidue
AGLU57
AGLU136
AASP140
ACO184
AHOH294
AHOH338
AHOH345
AHOH349
AHOH507

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CO A 184
ChainResidue
AHIS54
AASP140
ACO178
ACO183
AHOH344
AHOH345
AHOH347
AHOH349
AHOH491

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CO A 185
ChainResidue
AASP127
AHOH250
AHOH250
AHOH250
AHOH342
AHOH342
AHOH342

site_idBC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MG A 186
ChainResidue
AHOH361
AHOH361
AHOH379
AHOH379
AHOH392
AHOH392
AHOH406
AHOH406

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 187
ChainResidue
ASER10
AHOH235
AHOH376
AHOH440
AHOH444
AHOH493

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 188
ChainResidue
AHOH213
AHOH304
AHOH315
AHOH333
AHOH396
AHOH490

site_idBC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE CL A 189
ChainResidue
AHIS169
AHIS169
ACO176
ACO176
ACO176
ACO176
ALEU165
ALEU165
ALEU165
ALEU165
AHIS169
AHIS169

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL A 190
ChainResidue
ASER131
AGLU132
ATYR133
AGLU135
AGLU136
AHOH511

site_idBC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 191
ChainResidue
AHOH253
AHOH299
AHOH323
AHOH334
AHOH473
AHOH515

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 192
ChainResidue
AHOH340
AHOH341
AHOH414
AHOH461

site_idBC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 193
ChainResidue
AARG5
AASN7
ATYR8
AHOH302

site_idCC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 194
ChainResidue
ASER10
AHOH293

Functional Information from PROSITE/UniProt
site_idPS00204
Number of Residues21
DetailsFERRITIN_2 Ferritin iron-binding regions signature 2. DphLCDFLEseYLeeevkdIK
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 Residues149
DetailsDomain: {"description":"Ferritin-like diiron","evidences":[{"source":"PROSITE-ProRule","id":"PRU00085","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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