Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2Z5Q

Apo-Fr with intermediate content of Pd ion

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 PD A 201
ChainResidue
AGLU45
AHIS49
AHIS173

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PD A 202
ChainResidue
AASP38
AGLU45
ACYS48
AARG52

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PD A 203
ChainResidue
AARG52
AGLU45
AHIS49

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PD A 204
ChainResidue
AHIS114
ACYS126

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PD A 206
ChainResidue
ASER2
AGLN3
AASP40
AARG75

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PD A 207
ChainResidue
ASER118
ACYS126

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE PD A 208
ChainResidue
ACYS126

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PD A 209
ChainResidue
AGLU45
ACYS48
AHIS49
AARG52

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CD A 210
ChainResidue
AASP80
AHOH1113

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 301
ChainResidue
ATHR10
AGLU11
AALA14
AHOH1038

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 302
ChainResidue
AGLN79
AASP80
AGLN82
AHOH1024
AHOH1116

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

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon