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2V2N

Mutant R59M recombinant horse spleen apoferritin cocrystallized with haemin in acidic conditions

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 Residues4
DetailsBINDING SITE FOR RESIDUE CD A 1172
ChainResidue
AASP80
AASP80
AHOH2115
AHOH2115

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CD A 1002
ChainResidue
AASP127
AASP127
AASP127

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CD A 1173
ChainResidue
AGLU130
AGLU130

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CD A 1174
ChainResidue
AHIS114
ACYS126
AGLU130

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CD A 1175
ChainResidue
AASP38
ACYS48

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CD A 1176
ChainResidue
AGLU57
AGLU60

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CD A 1177
ChainResidue
AGLU11
AHOH2025
AHOH2027

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CD A 1178
ChainResidue
AGLU53
AGLU56

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 1179
ChainResidue
AHIS132
AASP135
AHOH2101

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 1180
ChainResidue
ATYR36
AVAL42
AGLY90
AARG153
AGLU163

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1181
ChainResidue
ALEU22
ASER105
AALA109
AHOH2199
AHOH2200
AHOH2201
AHOH2202

site_idBC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 1182
ChainResidue
AGLN6
AASN7
AHOH2009
AHOH2011
AHOH2019
AHOH2152
AHOH2203
AHOH2204

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
ALEU54
AGLU57
ALYS58
AGLY61
AARG64

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:7026284
ChainResidueDetails
ASER2

220113

PDB entries from 2024-05-22

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