4BXF

60S ribosomal protein L27A histidine hydroxylase (MINA53 Y209C) in complex with MN(II), 2-oxoglutarate (2OG) and 60S ribosomal protein L27A (RPL27A G37C) peptide fragment

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Functional Information from GO Data

ChainGOidnamespacecontents
A0005829cellular_componentcytosol
A0005730cellular_componentnucleolus
A0005654cellular_componentnucleoplasm
A0005634cellular_componentnucleus
A0005667cellular_componenttranscription factor complex
A0051213molecular_functiondioxygenase activity
A0032452molecular_functionhistone demethylase activity
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0042254biological_processribosome biogenesis
B0005829cellular_componentcytosol
B0005730cellular_componentnucleolus
B0005654cellular_componentnucleoplasm
B0005634cellular_componentnucleus
B0005667cellular_componenttranscription factor complex
B0051213molecular_functiondioxygenase activity
B0032452molecular_functionhistone demethylase activity
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B0042254biological_processribosome biogenesis
C0005829cellular_componentcytosol
C0022625cellular_componentcytosolic large ribosomal subunit
C0005783cellular_componentendoplasmic reticulum
C0016020cellular_componentmembrane
C0003723molecular_functionRNA binding
C0003735molecular_functionstructural constituent of ribosome
C0000184biological_processnuclear-transcribed mRNA catabolic process, nonsense-mediated decay
C0006614biological_processSRP-dependent cotranslational protein targeting to membrane
C0006412biological_processtranslation
C0006413biological_processtranslational initiation
D0005829cellular_componentcytosol
D0022625cellular_componentcytosolic large ribosomal subunit
D0005783cellular_componentendoplasmic reticulum
D0016020cellular_componentmembrane
D0003723molecular_functionRNA binding
D0003735molecular_functionstructural constituent of ribosome
D0000184biological_processnuclear-transcribed mRNA catabolic process, nonsense-mediated decay
D0006614biological_processSRP-dependent cotranslational protein targeting to membrane
D0006412biological_processtranslation
D0006413biological_processtranslational initiation
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Functional Information from PDB Data

site_idNumber of ResiduesDetails
AC15BINDING SITE FOR RESIDUE MN A 601
ChainResidue
AHIS179
AASP181
AHIS240
AAKG901
AHOH2098

AC212BINDING SITE FOR RESIDUE AKG A 901
ChainResidue
ATYR167
AHIS179
AASP181
ALYS194
AHIS240
AHIS253
ATHR255
AMN601
AHOH2098
AHOH2099
AHOH2106
AHOH2110

AC35BINDING SITE FOR RESIDUE MN B 601
ChainResidue
BHIS179
BASP181
BHIS240
BAKG901
BHOH2037

AC49BINDING SITE FOR RESIDUE AKG B 901
ChainResidue
BHIS179
BASP181
BLYS194
BHIS240
BHIS253
BTHR255
BMN601
BHOH2037
BHOH2038

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Functional Information from PDB atom coordinates for the "HETATM" binding sites

site_idNumber of ResiduesDetails
AKG_4bxf_A_901142-OXOGLUTARIC ACID binding site
ChainResidueligand
ATYR167AKG: 2-OXOGLUTARIC ACID
ATHR169AKG: 2-OXOGLUTARIC ACID
AGLY175-LEU176AKG: 2-OXOGLUTARIC ACID
AHIS179AKG: 2-OXOGLUTARIC ACID
AASP181AKG: 2-OXOGLUTARIC ACID
AILE187AKG: 2-OXOGLUTARIC ACID
ALYS194AKG: 2-OXOGLUTARIC ACID
ATRP196AKG: 2-OXOGLUTARIC ACID
AHIS240AKG: 2-OXOGLUTARIC ACID
AALA242AKG: 2-OXOGLUTARIC ACID
AHIS253AKG: 2-OXOGLUTARIC ACID
ATHR255AKG: 2-OXOGLUTARIC ACID
CHIS39AKG: 2-OXOGLUTARIC ACID

AKG_4bxf_B_901162-OXOGLUTARIC ACID binding site
ChainResidueligand
BTHR134AKG: 2-OXOGLUTARIC ACID
BTYR167AKG: 2-OXOGLUTARIC ACID
BTHR169AKG: 2-OXOGLUTARIC ACID
BGLY175-LEU176AKG: 2-OXOGLUTARIC ACID
BHIS179AKG: 2-OXOGLUTARIC ACID
BASP181AKG: 2-OXOGLUTARIC ACID
BILE187AKG: 2-OXOGLUTARIC ACID
BLYS194AKG: 2-OXOGLUTARIC ACID
BTRP196AKG: 2-OXOGLUTARIC ACID
BPHE234AKG: 2-OXOGLUTARIC ACID
BHIS240AKG: 2-OXOGLUTARIC ACID
BALA242AKG: 2-OXOGLUTARIC ACID
BHIS253AKG: 2-OXOGLUTARIC ACID
BTHR255AKG: 2-OXOGLUTARIC ACID
DHIS39AKG: 2-OXOGLUTARIC ACID

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Functional Information from PROSITE/UniProt

site_idNumber of ResiduesDetails
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Functional Information from SwissProt/UniProt

site_idNumber of ResiduesDetails
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Catalytic Information from CSA

site_idNumber of ResiduesDetails