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1HRS

A CRYSTALLOGRAPHIC STUDY OF HAEM BINDING TO FERRITIN

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
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
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD A 201
ChainResidue
AASP80
AASP80
AGLN82
AGLN82

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CD A 202
ChainResidue
AASP127
ACYS126
ACYS126
ACYS126
AASP127
AASP127

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE PP9 A 200
ChainResidue
ALEU24
ASER27
ASER27
ATYR28
ATYR28
ALEU31
ALEU31
AARG52
AARG52
AALA55
AALA55
AGLU56
AGLU56
AARG59
AARG59
AGLU60
AGLU63
AGLU63
ALEU81

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
ALEU54
AGLU57
ALYS58
AGLY61
AARG64

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:7026284
ChainResidueDetails
ASER2

218853

PDB entries from 2024-04-24

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