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1E93

High resolution structure and biochemical properties of a recombinant catalase depleted in iron

Functional Information from GO Data
ChainGOidnamespacecontents
A0004096molecular_functioncatalase activity
A0004601molecular_functionperoxidase activity
A0005737cellular_componentcytoplasm
A0006979biological_processresponse to oxidative stress
A0020037molecular_functionheme binding
A0042542biological_processresponse to hydrogen peroxide
A0042744biological_processhydrogen peroxide catabolic process
A0046872molecular_functionmetal ion binding
A0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT A 700
ChainResidue
AGLU38
AHIS42
AARG342
AHIS349
AHOH2423
AHOH2424
AHOH2610

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 800
ChainResidue
AHOH2533
AHOH2611
AHOH2612
AHOH2613
AHOH2614
AARG423
AHOH2358

site_idAC3
Number of Residues26
DetailsBINDING SITE FOR RESIDUE HEM A 600
ChainResidue
AASP44
AARG51
AHIS54
AARG91
AGLY110
APHE111
AVAL125
AGLY126
AASN127
APRO137
APHE140
AGLY195
ASER196
AHIS197
APHE313
AMET329
AARG333
ASER336
ATYR337
AALA340
AHIS341
AARG344
AHOH2138
AHOH2607
AHOH2608
AHOH2609

Functional Information from PROSITE/UniProt
site_idPS00437
Number of Residues9
DetailsCATALASE_1 Catalase proximal heme-ligand signature. RLFSYgDAH
ChainResidueDetails
AARG333-HIS341

site_idPS00438
Number of Residues17
DetailsCATALASE_2 Catalase proximal active site signature. FdRevipERrmHakGSG
ChainResidueDetails
APHE43-GLY59

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE:
ChainResidueDetails
AHIS54
AASN127

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:7791219
ChainResidueDetails
ATYR337

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Methionine sulfone => ECO:0000269|PubMed:7786407
ChainResidueDetails
AOMT53

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1iph
ChainResidueDetails
AHIS54
AASN127
ASER93

224004

PDB entries from 2024-08-21

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