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3NOZ

Crystal Structure of Pd(allyl)/apo-E45C/R52H-rHLFr

Functional Information from GO Data
ChainGOidnamespacecontents
X0005506molecular_functioniron ion binding
X0005737cellular_componentcytoplasm
X0006826biological_processiron ion transport
X0006879biological_processintracellular iron ion homeostasis
X0006880biological_processintracellular sequestering of iron ion
X0008043cellular_componentintracellular ferritin complex
X0008198molecular_functionferrous iron binding
X0008199molecular_functionferric iron binding
X0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 X 175
ChainResidue
XGLN6
XASN7
XHOH227
XHOH243
XHOH271

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD X 176
ChainResidue
XASP80
XASP80
XGLN82
XGLN82

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PLL X 180
ChainResidue
XHIS114
XPRO123
XCYS126
XCYS126
XLEU134

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PLL X 181
ChainResidue
XHIS114
XSER118
XPRO123
XCYS126
XHOH259
XHOH259
XHOH259

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PLL X 182
ChainResidue
XPHE35
XASP38
XCYS48
XPLL183
XHOH232

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PLL X 183
ChainResidue
XCYS48
XHIS49
XHIS52
XPLL182

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PLL X 184
ChainResidue
XCYS45
XHIS49
XHIS173
XPLL185

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PLL X 185
ChainResidue
XCYS45
XHIS173
XEDO177
XPLL184
XEDO191

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO X 177
ChainResidue
XGLU167
XARG168
XLEU171
XLYS172
XHIS173
XPLL185
XHOH275

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO X 178
ChainResidue
XGLN86
XGLU88
XGLY90
XASP94

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO X 179
ChainResidue
XTYR36
XASP41
XGLU88
XEDO186

site_idBC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO X 186
ChainResidue
XTYR36
XGLY90
XTHR91
XARG153
XGLU163
XEDO179
XHOH362

site_idBC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO X 187
ChainResidue
XILE151
XLEU154
XVAL155
XALA159
XGLY162
XGLU163
XPHE166
XHOH230
XHOH329

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO X 188
ChainResidue
XASN7
XTYR8
XSER9
XGLN120
XHOH236

site_idBC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO X 189
ChainResidue
XHIS52
XGLU63
XHOH298

site_idBC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO X 190
ChainResidue
XHOH224
XHOH226
XHOH309

site_idBC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO X 191
ChainResidue
XASP146
XARG168
XPLL185
XHOH233
XHOH325
XHOH326

Functional Information from PROSITE/UniProt
site_idPS00204
Number of Residues21
DetailsFERRITIN_2 Ferritin iron-binding regions signature 2. DphLCDFLEshFLdeevklIK
ChainResidueDetails
XASP122-LYS142

site_idPS00540
Number of Residues19
DetailsFERRITIN_1 Ferritin iron-binding regions signature 1. EkREgaERLLkmQNqRgGR
ChainResidueDetails
XGLU57-ARG75

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00085
ChainResidueDetails
XGLU53
XGLU56
XGLU57
XGLU60
XGLU63

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:7026284
ChainResidueDetails
XSER1

219869

PDB entries from 2024-05-15

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