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5XHO

Crystal structure of Frog M-ferritin E135K 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
AHOH317
AHOH416
AHOH426

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 202
ChainResidue
AHOH418
AHOH451
AHOH502
ASER10
AHOH369
AHOH398

site_idAC3
Number of Residues6
Detailsbinding site for residue MG A 203
ChainResidue
AHOH320
AHOH320
AHOH320
AHOH474
AHOH474
AHOH474

site_idAC4
Number of Residues7
Detailsbinding site for residue MG A 204
ChainResidue
AGLU103
AGLU136
AGLN137
AASP140
AMG206
AHOH314
AHOH321

site_idAC5
Number of Residues4
Detailsbinding site for residue MG A 205
ChainResidue
AHOH357
AHOH357
AHOH478
AHOH478

site_idAC6
Number of Residues6
Detailsbinding site for residue MG A 206
ChainResidue
AGLU136
AGLN137
AMG204
AHOH314
AHOH321
AHOH362

site_idAC7
Number of Residues3
Detailsbinding site for residue MG A 207
ChainResidue
AHOH521
AHOH521
AHOH521

site_idAC8
Number of Residues6
Detailsbinding site for residue MG A 208
ChainResidue
AHOH364
AHOH364
AHOH364
AHOH435
AHOH435
AHOH435

site_idAC9
Number of Residues4
Detailsbinding site for residue MG A 209
ChainResidue
AHOH424
AHOH491
AHOH492
AHOH503

site_idAD1
Number of Residues6
Detailsbinding site for residue MG A 210
ChainResidue
AGLU130
AGLU130
AGLU130
AHOH308
AHOH308
AHOH308

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 Residues3
Detailsbinding site for residue CL A 213
ChainResidue
AASP87
AGLU88
AHOH381

site_idAD5
Number of Residues2
Detailsbinding site for residue CL A 214
ChainResidue
ASER10
AHOH494

site_idAD6
Number of Residues4
Detailsbinding site for residue CL A 215
ChainResidue
AARG5
AASN7
ATYR8
AHOH464

site_idAD7
Number of Residues6
Detailsbinding site for residue CL A 216
ChainResidue
ASER131
AGLU132
ATYR133
ALYS135
AGLU136
AHOH470

site_idAD8
Number of Residues2
Detailsbinding site for residue CL A 217
ChainResidue
AASN150
ACL220

site_idAD9
Number of Residues3
Detailsbinding site for residue CL A 218
ChainResidue
AGLN101
ALEU102
ATHR105

site_idAE1
Number of Residues5
Detailsbinding site for residue CL A 219
ChainResidue
AASN7
AGLN108
ALYS115
AHOH325
AHOH439

site_idAE2
Number of Residues3
Detailsbinding site for residue CL A 220
ChainResidue
AASN150
ASER170
ACL217

site_idAE3
Number of Residues2
Detailsbinding site for residue CL A 221
ChainResidue
AASN159
AHOH347

site_idAE4
Number of Residues3
Detailsbinding site for residue CL A 222
ChainResidue
AASN7
AHOH325
AHOH523

site_idAE5
Number of Residues2
Detailsbinding site for residue CL A 223
ChainResidue
AARG75
AHOH401

Functional Information from PROSITE/UniProt
site_idPS00204
Number of Residues21
DetailsFERRITIN_2 Ferritin iron-binding regions signature 2. DphLCDFLEseYLkeqvkdIK
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
AHIS61
AGLU103
AGLN137
AASP140
AGLU23
AGLU58

221051

PDB entries from 2024-06-12

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