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5ERK

X-ray structure of horse spleen apoferritin (control)

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
A0006880biological_processintracellular sequestering of iron ion
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
ACL216
AHOH377
AHOH396

site_idAC2
Number of Residues3
Detailsbinding site for residue CD A 202
ChainResidue
AGLU53
AGLU56
AHOH340

site_idAC3
Number of Residues3
Detailsbinding site for residue CD A 203
ChainResidue
AHOH447
AGLU56
AGLU60

site_idAC4
Number of Residues2
Detailsbinding site for residue CD A 204
ChainResidue
AASP80
ACL215

site_idAC5
Number of Residues4
Detailsbinding site for residue CD A 205
ChainResidue
AARG39
AGLU88
AHOH313
AHOH441

site_idAC6
Number of Residues6
Detailsbinding site for residue CD A 206
ChainResidue
AASP127
AGLU130
ASER131
AHOH349
AHOH448
AHOH456

site_idAC7
Number of Residues6
Detailsbinding site for residue CD A 207
ChainResidue
AHIS132
AASP135
AHOH374
AHOH425
AHOH448
AHOH456

site_idAC8
Number of Residues6
Detailsbinding site for residue CD A 208
ChainResidue
AGLU130
AGLU130
AGLU130
ACL214
ACL214
ACL214

site_idAC9
Number of Residues6
Detailsbinding site for residue CD A 209
ChainResidue
AHIS114
ACYS126
AGLU130
ACL214
ACL214
AHOH480

site_idAD1
Number of Residues2
Detailsbinding site for residue CD A 210
ChainResidue
AARG59
AGLU63

site_idAD2
Number of Residues4
Detailsbinding site for residue CD A 211
ChainResidue
ACYS48
AHIS49
AARG52
AHOH465

site_idAD3
Number of Residues3
Detailsbinding site for residue CD A 212
ChainResidue
AGLU45
AHOH400
AHOH431

site_idAD4
Number of Residues3
Detailsbinding site for residue CD A 213
ChainResidue
AGLU45
AHIS49
AHOH373

site_idAD5
Number of Residues7
Detailsbinding site for residue CL A 214
ChainResidue
AGLU130
AGLU130
ACD208
ACD208
ACD208
ACD209
ACD209

site_idAD6
Number of Residues1
Detailsbinding site for residue CL A 215
ChainResidue
ACD204

site_idAD7
Number of Residues3
Detailsbinding site for residue CL A 216
ChainResidue
ASER9
ATHR10
ACD201

site_idAD8
Number of Residues5
Detailsbinding site for residue SO4 A 217
ChainResidue
AGLN6
AASN7
AHOH301
AHOH329
AHOH413

site_idAD9
Number of Residues6
Detailsbinding site for residue GOL A 218
ChainResidue
AGLN3
ALYS104
ALEU148
AHOH316
AHOH360
AHOH409

site_idAE1
Number of Residues3
Detailsbinding site for residue GOL A 219
ChainResidue
AGLY90
AGLU163
AHOH302

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

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PDB entries from 2024-07-10

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