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3KXU

Crystal structure of human ferritin FTL498InsTC pathogenic mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006826biological_processiron ion transport
A0006879biological_processintracellular iron ion homeostasis
A0006880biological_processintracellular sequestering of iron ion
A0008043cellular_componentintracellular ferritin complex
A0008198molecular_functionferrous iron binding
A0008199molecular_functionferric iron binding
A0016020cellular_componentmembrane
A0035578cellular_componentazurophil granule lumen
A0042802molecular_functionidentical protein binding
A0044754cellular_componentautolysosome
A0046872molecular_functionmetal ion binding
A0055072biological_processobsolete iron ion homeostasis
A0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CD A 301
ChainResidue
AHIS115
ACYS127
AHOH192
AHOH193
AHOH194
AHOH215

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD A 302
ChainResidue
ACD304
AHIS50
AGLU54
AHOH220

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CD A 304
ChainResidue
AHIS50
ACD302

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CD A 305
ChainResidue
AGLU54
AGLU57
AHOH221
AHOH222
AHOH223

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD A 306
ChainResidue
AGLU58
AGLU61
AHOH224
AHOH225

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CD A 308
ChainResidue
AGLU89
AHOH226
AHOH227

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CD A 309
ChainResidue
AHIS133
AHOH228
AHOH229
AHOH230
AHOH231
AHOH232

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD A 312
ChainResidue
AGLU87
AHOH233
AHOH234
AHOH235

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD A 313
ChainResidue
ACYS127
AASP128
AGLU131
AGLU131

site_idBC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CD A 314
ChainResidue
AASP128

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CD A 315
ChainResidue
AASP12
AASP12
AHOH236
AHOH236
AHOH237
AHOH237

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CD A 316
ChainResidue
AHIS153
AHOH238
AHOH239

site_idBC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 317
ChainResidue
ASER10
AASP12
AARG121
AARG121
AHOH237
AHOH345
AHOH346
AHOH381
AHOH419
AHOH423

Functional Information from PROSITE/UniProt
site_idPS00204
Number of Residues21
DetailsFERRITIN_2 Ferritin iron-binding regions signature 2. DphLCDFLEthFLdeevklIK
ChainResidueDetails
AASP123-LYS143

site_idPS00540
Number of Residues19
DetailsFERRITIN_1 Ferritin iron-binding regions signature 1. EkREgyERLLkmQNqRgGR
ChainResidueDetails
AGLU58-ARG76

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING:
ChainResidueDetails
AGLU54
AGLU57
AGLU58
AGLU61
AGLU64

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:6653779
ChainResidueDetails
ASER2

218853

PDB entries from 2024-04-24

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