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2ZG9

Crystal Structure of Pd(allyl)/apo-H114AFr

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 Residues3
DetailsBINDING SITE FOR RESIDUE CD X 175
ChainResidue
XASP80
XGLN82
XHOH286

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 X 176
ChainResidue
XGLN86
XASP87
XGLU88
XHOH255
XHOH391

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 X 177
ChainResidue
XASP146
XHIS147
XHOH209
XHOH266
XHOH268
XHOH311
XHOH335
XLYS143

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 X 178
ChainResidue
XGLN6
XASN7
XHOH227
XHOH259
XHOH264
XHOH284

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 X 179
ChainResidue
XGLU45
XHIS49
XARG168
XHIS173
XHOH311
XHOH359

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PLL X 180
ChainResidue
XCYS126
XGLU130

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PLL X 181
ChainResidue
XASP38
XGLU45
XCYS48
XLYS67

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PLL X 182
ChainResidue
XCYS48
XHIS49
XARG52

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO X 183
ChainResidue
XTYR36
XGLY90
XTHR91
XARG153
XGLU163
XHOH276
XHOH330

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO X 184
ChainResidue
XALA14
XASN17
XARG18
XHOH238
XHOH252
XHOH332

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO X 185
ChainResidue
XTHR10
XGLU11
XALA14
XHOH210
XHOH293
XHOH322

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO X 186
ChainResidue
XARG25
XGLN82
XLYS83
XSER85
XHOH298
XHOH390

site_idBC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO X 187
ChainResidue
XHIS49
XHOH359

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO X 188
ChainResidue
XSER27
XGLU56
XARG59
XHOH305

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 2024-07-24

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