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3O7R

Crystal structure of Ru(p-cymene)/apo-H49AFr

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
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 175
ChainResidue
AASP80
AASP80
AHOH225
AHOH225

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CD A 176
ChainResidue
AGLU60

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD A 177
ChainResidue
AASP38
AGLU45
AHOH346
AHOH367

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE RU A 178
ChainResidue
AHIS114
ACYS126
AGLU130
AHOH370

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE RU A 179
ChainResidue
AHIS173

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 180
ChainResidue
AGLN6
AASN7
AHOH237
AHOH254
AHOH300

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 181
ChainResidue
ALYS143
AASP146
AEDO188
AHOH216
AHOH222
AHOH263

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 182
ChainResidue
ASER27
AARG59

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 183
ChainResidue
AARG5
ATYR8
ATHR10
AHOH237

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 184
ChainResidue
ASER85
AGLN86
AHOH261
AHOH311

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 186
ChainResidue
AGLY90
AHOH282

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 187
ChainResidue
ALEU77
AASP87
AHOH217

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 188
ChainResidue
AGLU45
AARG168
ALYS172
ASO4181
AHOH238

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 Residues149
DetailsDomain: {"description":"Ferritin-like diiron","evidences":[{"source":"PROSITE-ProRule","id":"PRU00085","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues7
DetailsRegion: {"description":"Catalytic site for iron oxidation"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00085","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"7026284","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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