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2ZG7

Crystal Structure of Pd(allyl)/apo-Fr

Functional Information from GO Data
ChainGOidnamespacecontents
X0005506molecular_functioniron ion binding
X0005737cellular_componentcytoplasm
X0005764cellular_componentlysosome
X0005776cellular_componentautophagosome
X0006826biological_processiron ion transport
X0006879biological_processintracellular iron ion homeostasis
X0006880biological_processintracellular sequestering of iron ion
X0008198molecular_functionferrous iron binding
X0008199molecular_functionferric iron binding
X0031410cellular_componentcytoplasmic vesicle
X0044754cellular_componentautolysosome
X0046872molecular_functionmetal ion binding
X0070288cellular_componentferritin complex
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CD X 175
ChainResidue
XASP80
XHOH220

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 X 176
ChainResidue
XGLN6
XASN7
XHOH228
XHOH253
XHOH255
XHOH263
XHOH383

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 X 177
ChainResidue
XGLU45
XLYS143
XASP146
XHIS147
XHOH210
XHOH274
XHOH330
XHOH361
XHOH411

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 X 178
ChainResidue
XGLU45
XHIS49
XARG168
XHIS173
XHOH244
XHOH411

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 X 179
ChainResidue
XGLN86
XASP87
XGLU88
XHOH281
XHOH289
XHOH413

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PLL X 180
ChainResidue
XHIS114
XPRO123
XCYS126
XGLU130
XHOH404

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PLL X 181
ChainResidue
XPRO123
XCYS126
XHOH404

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PLL X 182
ChainResidue
XASP38
XGLU45
XCYS48

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PLL X 183
ChainResidue
XCYS48
XHIS49
XARG52

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO X 184
ChainResidue
XTYR36
XGLY90
XTHR91
XGLU163
XHOH329

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO X 185
ChainResidue
XTHR10
XGLU11
XHOH236
XHOH307
XHOH359

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO X 186
ChainResidue
XASP127
XPHE128
XHIS132
XASP135
XHOH277

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO X 187
ChainResidue
XSER27
XARG59
XHOH380

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO X 188
ChainResidue
XARG5
XTYR8
XTHR10
XHOH228

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO X 189
ChainResidue
XTYR36
XARG39
XASP41
XGLU88

site_idBC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO X 190
ChainResidue
XSER85
XGLN86
XHOH412

site_idBC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO X 191
ChainResidue
XSER1
XHOH260

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

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PDB entries from 2024-07-10

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