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3WVW

Crystal structure of RuCO/apo-WTFr

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
A0005764cellular_componentlysosome
A0005776cellular_componentautophagosome
A0006826biological_processiron ion transport
A0006879biological_processintracellular iron ion homeostasis
A0006880biological_processintracellular sequestering of iron ion
A0008198molecular_functionferrous iron binding
A0008199molecular_functionferric iron binding
A0031410cellular_componentcytoplasmic vesicle
A0044754cellular_componentautolysosome
A0046872molecular_functionmetal ion binding
A0070288cellular_componentferritin complex
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CD A 201
ChainResidue
AGLU130
AGLU130
AGLU130

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CD A 202
ChainResidue
AASP127
AASP127
AASP127

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD A 203
ChainResidue
AGLN82
AASP80
AASP80
AGLN82

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 204
ChainResidue
AGLN6
AASN7
AHOH332
AHOH353
AHOH392
AHOH411

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 205
ChainResidue
AGLU60
AARG64
AHIS132
AEDO208
AHOH364

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 206
ChainResidue
ATYR36
AGLY90
ATHR91
AARG153
AGLU163
AHOH416

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 207
ChainResidue
APHE50
AGLU53
AGLU57
ALEU140
ALYS143

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 208
ChainResidue
ATYR23
AGLU57
ALYS58
AGLU137
AEDO205
AHOH320

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 209
ChainResidue
ATHR91
ATHR92
ALEU93
AGLU163
AHOH398

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 210
ChainResidue
AHIS114
ASER118
AALA121
ARU213
AHOH319

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 211
ChainResidue
AASP112
ALEU113
AHOH339
AHOH355

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 212
ChainResidue
ALYS104
ASER105
AHOH338

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE RU A 213
ChainResidue
AHIS114
ACYS126
AGLU130
AEDO210

site_idBC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE RU A 214
ChainResidue
AHIS132

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE RU1 A 215
ChainResidue
AASP38
AGLU45
ACYS48
AHOH367

Functional Information from PROSITE/UniProt
site_idPS00204
Number of Residues21
DetailsFERRITIN_2 Ferritin iron-binding regions signature 2. DphLCDFLEshFLdeevklIK
ChainResidueDetails
AASP122-LYS142

site_idPS00540
Number of Residues19
DetailsFERRITIN_1 Ferritin iron-binding regions signature 1. EkREgaERLLkmQNqRgGR
ChainResidueDetails
AGLU57-ARG75

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00085
ChainResidueDetails
AGLU53
AGLU56
AGLU57
AGLU60
AGLU63

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:7026284
ChainResidueDetails
ASER1

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PDB entries from 2024-07-24

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