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6HJT

The X-ray structure of the horse spleen ferritin nanocage containing Pt, obtained upon encapsulation of a Pt(II) terpyridine compound within the protein cage

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 Residues3
Detailsbinding site for residue CD A 201
ChainResidue
AGLU11
ACL209
AHOH329

site_idAC2
Number of Residues3
Detailsbinding site for residue CD A 202
ChainResidue
AGLU53
AGLU56
AHOH309

site_idAC3
Number of Residues3
Detailsbinding site for residue CD A 203
ChainResidue
AGLU56
AGLU60
AHOH307

site_idAC4
Number of Residues4
Detailsbinding site for residue CD A 204
ChainResidue
AASP80
AASP80
ACL208
ACL208

site_idAC5
Number of Residues4
Detailsbinding site for residue CD A 205
ChainResidue
ACYS48
AHIS49
AARG52
ACL218

site_idAC6
Number of Residues6
Detailsbinding site for residue CD A 206
ChainResidue
AGLU130
AGLU130
AGLU130
AHOH363
AHOH363
AHOH363

site_idAC7
Number of Residues9
Detailsbinding site for residue CD A 207
ChainResidue
AASP127
AASP127
AASP127
AHOH318
AHOH318
AHOH318
AHOH496
AHOH496
AHOH496

site_idAC8
Number of Residues5
Detailsbinding site for residue CL A 208
ChainResidue
AASP80
AGLN82
ALYS83
ACD204
ACD204

site_idAC9
Number of Residues5
Detailsbinding site for residue CL A 209
ChainResidue
ASER9
ATHR10
AGLU11
ACD201
AHOH517

site_idAD1
Number of Residues4
Detailsbinding site for residue PT A 210
ChainResidue
AHIS49
AHOH304
AHOH474
AHOH527

site_idAD2
Number of Residues4
Detailsbinding site for residue PT A 211
ChainResidue
AHIS132
AHOH311
AHOH378
AHOH519

site_idAD3
Number of Residues4
Detailsbinding site for residue PT A 212
ChainResidue
AHIS49
ACL218
AHOH334
AHOH422

site_idAD4
Number of Residues3
Detailsbinding site for residue PT A 213
ChainResidue
AHIS132
ADMS217
AHOH438

site_idAD5
Number of Residues4
Detailsbinding site for residue PT A 214
ChainResidue
AHIS114
ACYS126
AGLU130
AHOH363

site_idAD6
Number of Residues5
Detailsbinding site for residue SO4 A 215
ChainResidue
AGLN6
AASN7
AHOH303
AHOH324
AHOH330

site_idAD7
Number of Residues3
Detailsbinding site for residue GOL A 216
ChainResidue
ASER27
ASER27
AHOH415

site_idAD8
Number of Residues4
Detailsbinding site for residue DMS A 217
ChainResidue
AHIS132
AASP135
APT213
AHOH308

site_idAD9
Number of Residues4
Detailsbinding site for residue CL A 218
ChainResidue
AGLU45
ACD205
APT212
AHOH367

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

221051

PDB entries from 2024-06-12

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