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7BON

Crystal structure of recombinant horse spleen apo-R52C/E56C/R59C/E63C-Fr

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
A0006826biological_processiron ion transport
A0006879biological_processintracellular iron ion homeostasis
A0006880biological_processintracellular sequestering of iron ion
A0008043cellular_componentintracellular ferritin complex
A0008198molecular_functionferrous iron binding
A0008199molecular_functionferric iron binding
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue SO4 A 201
ChainResidue
AGLN6
AASN7
AHOH312
AHOH317
AHOH376
AHOH380

site_idAC2
Number of Residues4
Detailsbinding site for residue CD A 202
ChainResidue
ACL220
AASP80
AASP80
ACL220

site_idAC3
Number of Residues4
Detailsbinding site for residue CD A 203
ChainResidue
AASP38
AGLU45
ACYS48
AHOH446

site_idAC4
Number of Residues4
Detailsbinding site for residue CD A 204
ChainResidue
ACYS48
ACYS52
AHOH359
AHOH478

site_idAC5
Number of Residues3
Detailsbinding site for residue CD A 205
ChainResidue
ACYS59
ACYS63
AHOH441

site_idAC6
Number of Residues5
Detailsbinding site for residue CD A 206
ChainResidue
AHIS114
ACYS126
AGLU130
ACD210
AHOH301

site_idAC7
Number of Residues6
Detailsbinding site for residue CD A 207
ChainResidue
AGLU130
AGLU130
ACD210
ACD210
ACD210
AHOH301

site_idAC8
Number of Residues6
Detailsbinding site for residue CD A 208
ChainResidue
AHOH305
AHOH305
AHOH305
AHOH307
AHOH307
AHOH307

site_idAC9
Number of Residues2
Detailsbinding site for residue CD A 209
ChainResidue
AHIS132
ACD215

site_idAD1
Number of Residues6
Detailsbinding site for residue CD A 210
ChainResidue
AGLU130
ACD206
ACD207
ACD207
ACD207
AHOH301

site_idAD2
Number of Residues2
Detailsbinding site for residue CD A 211
ChainResidue
AHIS49
AGLU53

site_idAD3
Number of Residues2
Detailsbinding site for residue CD A 212
ChainResidue
AGLU57
AGLU60

site_idAD4
Number of Residues2
Detailsbinding site for residue CD A 213
ChainResidue
AGLU45
AHIS49

site_idAD5
Number of Residues1
Detailsbinding site for residue CD A 214
ChainResidue
ACYS63

site_idAD6
Number of Residues4
Detailsbinding site for residue CD A 215
ChainResidue
AHIS132
AASP135
ACD209
AHOH431

site_idAD7
Number of Residues3
Detailsbinding site for residue CD A 216
ChainResidue
AGLU11
AHOH418
AHOH437

site_idAD8
Number of Residues3
Detailsbinding site for residue CD A 217
ChainResidue
AGLU60
AHOH325
AHOH428

site_idAD9
Number of Residues7
Detailsbinding site for residue EDO A 218
ChainResidue
ATYR36
AGLY90
ATHR91
AARG153
AGLU163
AHOH364
AHOH366

site_idAE1
Number of Residues5
Detailsbinding site for residue EDO A 219
ChainResidue
AARG39
AARG75
AGLU88
AHOH318
AHOH351

site_idAE2
Number of Residues4
Detailsbinding site for residue CL A 220
ChainResidue
AASP80
AASP80
ACD202
ACD202

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00085
ChainResidueDetails
AGLU53
ACYS56
AGLU57
AGLU60
ACYS63

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

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PDB entries from 2024-06-12

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