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2B3X

Structure of an orthorhombic crystal form of human cytosolic aconitase (IRP1)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000900molecular_functionmRNA regulatory element binding translation repressor activity
A0003723molecular_functionRNA binding
A0003994molecular_functionaconitate hydratase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005783cellular_componentendoplasmic reticulum
A0005794cellular_componentGolgi apparatus
A0005829cellular_componentcytosol
A0006099biological_processtricarboxylic acid cycle
A0006101biological_processcitrate metabolic process
A0006740biological_processNADPH regeneration
A0006879biological_processintracellular iron ion homeostasis
A0010040biological_processresponse to iron(II) ion
A0016829molecular_functionlyase activity
A0017148biological_processnegative regulation of translation
A0030350molecular_functioniron-responsive element binding
A0046872molecular_functionmetal ion binding
A0051536molecular_functioniron-sulfur cluster binding
A0051538molecular_function3 iron, 4 sulfur cluster binding
A0051539molecular_function4 iron, 4 sulfur cluster binding
A0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1001
ChainResidue
AHIS408
AASP411
AHIS412
AHOH1161

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SF4 A 1000
ChainResidue
ACYS503
ACYS506
AASN535
AHOH1149
AILE176
AHIS178
AHIS207
ASER436
ACYS437

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 1002
ChainResidue
AASN133
ATYR417
APRO465
AILE467

Functional Information from PROSITE/UniProt
site_idPS00450
Number of Residues17
DetailsACONITASE_1 Aconitase family signature 1. VviAaITSC.TNTsnpsV
ChainResidueDetails
AVAL429-VAL445

site_idPS01244
Number of Residues14
DetailsACONITASE_2 Aconitase family signature 2. GfdVvgyGCMTCIG
ChainResidueDetails
AGLY495-GLY508

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues7
DetailsAnnotated By Reference To The Literature 1fgh
ChainResidueDetails
AGLU302
AHIS207
AHIS126
ASER778
AHIS178
AASP125
AASP205

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PDB entries from 2025-12-17

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