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5XHM

Crystal structure of Frog M-ferritin D40A 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
AHOH318
AHOH429
AHOH441

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 202
ChainResidue
AHOH439
AHOH465
AHOH527
ASER10
AHOH398
AHOH405

site_idAC3
Number of Residues6
Detailsbinding site for residue MG A 203
ChainResidue
AHOH359
AHOH364
AHOH376
AHOH453
AHOH529
AHOH560

site_idAC4
Number of Residues6
Detailsbinding site for residue MG A 204
ChainResidue
AHOH343
AHOH343
AHOH343
AHOH488
AHOH488
AHOH488

site_idAC5
Number of Residues6
Detailsbinding site for residue MG A 205
ChainResidue
AHOH312
AHOH312
AHOH312
AHOH325
AHOH325
AHOH325

site_idAC6
Number of Residues4
Detailsbinding site for residue MG A 206
ChainResidue
AHOH354
AHOH354
AHOH496
AHOH496

site_idAC7
Number of Residues7
Detailsbinding site for residue MG A 207
ChainResidue
AHIS61
AGLU136
AGLN137
AHOH311
AHOH313
AHOH353
AHOH357

site_idAC8
Number of Residues3
Detailsbinding site for residue MG A 208
ChainResidue
AHOH552
AHOH552
AHOH552

site_idAC9
Number of Residues4
Detailsbinding site for residue MG A 209
ChainResidue
AHIS169
AHIS169
AHIS169
AHIS169

site_idAD1
Number of Residues4
Detailsbinding site for residue MG A 210
ChainResidue
AHIS169
AHIS169
AHIS169
AHIS169

site_idAD2
Number of Residues2
Detailsbinding site for residue CL A 211
ChainResidue
ASER10
AHOH525

site_idAD3
Number of Residues3
Detailsbinding site for residue CL A 212
ChainResidue
AARG5
AASN7
ATYR8

site_idAD4
Number of Residues3
Detailsbinding site for residue CL A 213
ChainResidue
AASP87
AHOH320
AHOH546

site_idAD5
Number of Residues2
Detailsbinding site for residue CL A 214
ChainResidue
AASN150
AHOH341

site_idAD6
Number of Residues2
Detailsbinding site for residue CL A 215
ChainResidue
AASN159
AHOH344

site_idAD7
Number of Residues6
Detailsbinding site for residue CL A 216
ChainResidue
ASER131
AGLU132
ATYR133
AGLU135
AGLU136
AHOH516

site_idAD8
Number of Residues4
Detailsbinding site for residue CL A 217
ChainResidue
AVAL1
ASER2
AARG5
AGLY73

site_idAD9
Number of Residues4
Detailsbinding site for residue CL A 218
ChainResidue
AARG59
AARG59
AHOH379
AHOH379

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
AHIS61
AGLU103
AGLN137
AASP140
AGLU23
AGLU58

221051

PDB entries from 2024-06-12

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