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5E2D

Crystal structure of IrCp*/Pd(allyl)-apo-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 Residues3
Detailsbinding site for residue IR3 A 201
ChainResidue
AHIS49
AIR3202
AIR3205

site_idAC2
Number of Residues3
Detailsbinding site for residue IR3 A 202
ChainResidue
AHIS49
AIR3201
AIR3205

site_idAC3
Number of Residues1
Detailsbinding site for residue IR3 A 203
ChainResidue
APHE128

site_idAC4
Number of Residues4
Detailsbinding site for residue IR3 A 204
ChainResidue
ACYS126
APD211
AHIS114
ASER118

site_idAC5
Number of Residues3
Detailsbinding site for residue IR3 A 205
ChainResidue
AHIS49
AIR3201
AIR3202

site_idAC6
Number of Residues1
Detailsbinding site for residue IR A 206
ChainResidue
AHOH339

site_idAC7
Number of Residues8
Detailsbinding site for residue SO4 A 207
ChainResidue
AGLU45
ALYS143
AASP146
AHIS147
AHOH315
AHOH325
AHOH328
AHOH382

site_idAC8
Number of Residues5
Detailsbinding site for residue SO4 A 208
ChainResidue
AGLN6
AASN7
AHOH301
AHOH303
AHOH334

site_idAC9
Number of Residues5
Detailsbinding site for residue PLL A 209
ChainResidue
AGLU45
ACYS48
AHIS49
AARG52
APLL210

site_idAD1
Number of Residues4
Detailsbinding site for residue PLL A 210
ChainResidue
AASP38
AGLU45
ACYS48
APLL209

site_idAD2
Number of Residues3
Detailsbinding site for residue PD A 211
ChainResidue
AHIS114
ACYS126
AIR3204

site_idAD3
Number of Residues4
Detailsbinding site for residue CD A 212
ChainResidue
AASP80
AASP80
AGLN82
AGLN82

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

218853

PDB entries from 2024-04-24

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