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5MIJ

X-ray structure of carboplatin-encapsulated horse spleen apoferritin

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
A0005764cellular_componentlysosome
A0005776cellular_componentautophagosome
A0006826biological_processiron ion transport
A0006879biological_processintracellular iron ion homeostasis
A0008198molecular_functionferrous iron binding
A0008199molecular_functionferric iron binding
A0031410cellular_componentcytoplasmic vesicle
A0044754cellular_componentautolysosome
A0046872molecular_functionmetal ion binding
A0070288cellular_componentferritin complex
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue CD A 201
ChainResidue
AGLU11
ACL213
AHOH311
AHOH384

site_idAC2
Number of Residues3
Detailsbinding site for residue CD A 202
ChainResidue
AGLU53
AGLU56
AHOH315

site_idAC3
Number of Residues4
Detailsbinding site for residue CD A 203
ChainResidue
AGLU60
ACL218
AGLU56
AGLU57

site_idAC4
Number of Residues2
Detailsbinding site for residue CD A 204
ChainResidue
AASP80
ACL212

site_idAC5
Number of Residues4
Detailsbinding site for residue CD A 205
ChainResidue
AGLU88
AHOH307
AHOH420
AHOH428

site_idAC6
Number of Residues6
Detailsbinding site for residue CD A 206
ChainResidue
AGLU130
AGLU130
AGLU130
ACL211
ACL211
ACL211

site_idAC7
Number of Residues4
Detailsbinding site for residue CD A 207
ChainResidue
AHIS114
ACYS126
AGLU130
AHOH531

site_idAC8
Number of Residues4
Detailsbinding site for residue CD A 208
ChainResidue
ACYS48
AHIS49
AARG52
AHOH533

site_idAC9
Number of Residues3
Detailsbinding site for residue CD A 209
ChainResidue
AGLU45
ACD210
AHOH481

site_idAD1
Number of Residues2
Detailsbinding site for residue CD A 210
ChainResidue
AGLU45
ACD209

site_idAD2
Number of Residues5
Detailsbinding site for residue CL A 211
ChainResidue
AGLU130
AGLU130
ACD206
ACD206
ACD206

site_idAD3
Number of Residues2
Detailsbinding site for residue CL A 212
ChainResidue
AASP80
ACD204

site_idAD4
Number of Residues6
Detailsbinding site for residue CL A 213
ChainResidue
ASER9
ATHR10
AGLU11
ACD201
AHOH479
AHOH540

site_idAD5
Number of Residues1
Detailsbinding site for residue CD A 214
ChainResidue
AASP127

site_idAD6
Number of Residues7
Detailsbinding site for residue SO4 A 215
ChainResidue
AGLN6
AASN7
AHOH304
AHOH313
AHOH323
AHOH408
AHOH439

site_idAD7
Number of Residues1
Detailsbinding site for residue PT A 216
ChainResidue
AHIS132

site_idAD8
Number of Residues3
Detailsbinding site for residue PT A 217
ChainResidue
AGLU45
AHIS49
AGLU53

site_idAD9
Number of Residues3
Detailsbinding site for residue CL A 218
ChainResidue
AGLU57
AGLU60
ACD203

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

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00085
ChainResidueDetails
AGLU53
AGLU56
AGLU57
AGLU60
AGLU63

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:7026284
ChainResidueDetails
ASER1

227344

PDB entries from 2024-11-13

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