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3NP2

Crystal Structure of Pd(allyl)/apo-E45C/C48A-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 Residues6
DetailsBINDING SITE FOR RESIDUE SO4 X 175
ChainResidue
XGLN6
XASN7
XHOH221
XHOH271
XHOH283
XHOH284

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PLL X 176
ChainResidue
XCYS126
XGLU130
XPLL177
XHIS114
XPRO123
XCYS126

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PLL X 177
ChainResidue
XSER118
XPRO123
XCYS126
XPLL176
XHOH345
XHOH345

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PD X 178
ChainResidue
XCYS45
XHIS49
XPD179

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PD X 179
ChainResidue
XCYS45
XHIS173
XPD178

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD X 180
ChainResidue
XASP80
XASP80
XHOH257
XHOH257

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CD X 181
ChainResidue
XGLU56
XGLU60

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO X 182
ChainResidue
XALA109
XASP112
XLEU113
XHOH272
XHOH273
XHOH334

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO X 183
ChainResidue
XTHR10
XGLU11
XALA14
XHOH289

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO X 184
ChainResidue
XARG64
XHIS132

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO X 185
ChainResidue
XTYR36
XASP41
XVAL42

site_idBC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO X 186
ChainResidue
XGLN86

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO X 187
ChainResidue
XLYS143
XASP146
XARG168
XHOH225

site_idBC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO X 188
ChainResidue
XGLN3
XTHR149
XGLN152
XHOH280
XHOH346
XHOH347

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO X 189
ChainResidue
XVAL101
XLEU102
XSER105
XHOH217
XHOH244

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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