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5XHN

Crystal structure of Frog M-ferritin K104E mutant

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 Residues6
Detailsbinding site for residue MG A 201
ChainResidue
AGLU57
AGLU136
AASP140
AHOH321
AHOH451
AHOH462

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 202
ChainResidue
AHOH442
AHOH457
AHOH541
ASER10
AHOH391
AHOH393

site_idAC3
Number of Residues6
Detailsbinding site for residue MG A 203
ChainResidue
AHOH327
AHOH329
AHOH369
AHOH425
AHOH529
AHOH559

site_idAC4
Number of Residues6
Detailsbinding site for residue MG A 204
ChainResidue
AHOH359
AHOH359
AHOH359
AHOH491
AHOH491
AHOH491

site_idAC5
Number of Residues7
Detailsbinding site for residue MG A 205
ChainResidue
AGLU103
AGLU136
AGLN137
AASP140
AMG207
AHOH311
AHOH326

site_idAC6
Number of Residues3
Detailsbinding site for residue MG A 206
ChainResidue
AHOH558
AHOH558
AHOH558

site_idAC7
Number of Residues6
Detailsbinding site for residue MG A 207
ChainResidue
AGLU136
AGLN137
AMG205
AHOH311
AHOH326
AHOH370

site_idAC8
Number of Residues4
Detailsbinding site for residue MG A 208
ChainResidue
AASP127
AHOH340
AHOH340
AHOH340

site_idAC9
Number of Residues4
Detailsbinding site for residue MG A 209
ChainResidue
AHOH338
AHOH338
AHOH498
AHOH498

site_idAD1
Number of Residues6
Detailsbinding site for residue MG A 210
ChainResidue
AHOH420
AHOH503
AHOH513
AHOH519
AHOH563
AHOH566

site_idAD2
Number of Residues4
Detailsbinding site for residue MG A 211
ChainResidue
AHIS169
AHIS169
AHIS169
AHIS169

site_idAD3
Number of Residues4
Detailsbinding site for residue MG A 212
ChainResidue
AHIS169
AHIS169
AHIS169
AHIS169

site_idAD4
Number of Residues2
Detailsbinding site for residue CL A 213
ChainResidue
ASER10
AHOH523

site_idAD5
Number of Residues3
Detailsbinding site for residue CL A 214
ChainResidue
AARG5
AASN7
ATYR8

site_idAD6
Number of Residues4
Detailsbinding site for residue CL A 215
ChainResidue
AASP87
AGLU88
AHOH322
AHOH564

site_idAD7
Number of Residues6
Detailsbinding site for residue CL A 216
ChainResidue
ASER131
AGLU132
ATYR133
AGLU135
AGLU136
AHOH524

site_idAD8
Number of Residues3
Detailsbinding site for residue CL A 217
ChainResidue
AASP146
AASN150
ACL220

site_idAD9
Number of Residues2
Detailsbinding site for residue CL A 218
ChainResidue
AASN159
AHOH372

site_idAE1
Number of Residues4
Detailsbinding site for residue CL A 219
ChainResidue
AASN7
AGLN108
AHOH367
AHOH448

site_idAE2
Number of Residues4
Detailsbinding site for residue CL A 220
ChainResidue
AASN150
ASER170
ACL217
AHOH365

site_idAE3
Number of Residues3
Detailsbinding site for residue CL A 221
ChainResidue
AASN21
AHOH549
AHOH550

site_idAE4
Number of Residues3
Detailsbinding site for residue CL A 222
ChainResidue
AARG153
AGLU163
AHOH435

site_idAE5
Number of Residues3
Detailsbinding site for residue CL A 223
ChainResidue
ALYS82
AHOH383
AHOH443

Functional Information from PROSITE/UniProt
site_idPS00204
Number of Residues21
DetailsFERRITIN_2 Ferritin iron-binding regions signature 2. DphLCDFLEseYLeeqvkdIK
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
AGLN137
AASP140

221716

PDB entries from 2024-06-26

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