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2ZUR

Crystal Structure of Rh(nbd)/apo-Fr

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 Residues4
DetailsBINDING SITE FOR RESIDUE CD X 175
ChainResidue
XASP80
XASP80
XHOH349
XHOH349

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CD X 176
ChainResidue
XGLU60
XHOH381

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CD X 177
ChainResidue
XGLU11
XHOH236

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CD X 178
ChainResidue
XASP127
XASP127
XASP127

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CD X 179
ChainResidue
XRH183
XRH183

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 X 180
ChainResidue
XGLN6
XASN7
XHOH235
XHOH259
XHOH289
XHOH311
XHOH375

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 X 181
ChainResidue
XGLN86
XASP87
XGLU88
XHOH383

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE RH X 182
ChainResidue
XHIS49

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE RH X 183
ChainResidue
XHIS114
XCYS126
XCD179
XCD179
XHOH192

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO X 184
ChainResidue
XLEU93
XGLN152
XVAL155
XHOH264
XHOH315
XHOH324

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO X 185
ChainResidue
XTYR36
XGLY90
XTHR91
XARG153
XGLU163
XEDO190
XHOH293

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO X 186
ChainResidue
XSER85
XGLN86
XHOH266
XHOH344

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO X 187
ChainResidue
XGLU11
XALA14
XARG18
XHOH377
XHOH378

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO X 188
ChainResidue
XGLU45
XARG168
XLYS172
XHOH363

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO X 189
ChainResidue
XASP127
XSER131
XHIS132
XASP135

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO X 190
ChainResidue
XTYR36
XARG39
XASP41
XEDO185

site_idBC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO X 191
ChainResidue
XPHE37
XASP38
XALA43
XLEU44
XGLU45
XASP146
XHOH208
XHOH287
XHOH358

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

219140

PDB entries from 2024-05-01

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