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1MQF

Compound I from Proteus mirabilis catalase

Replaces:  2CAF
Functional Information from GO Data
ChainGOidnamespacecontents
A0004096molecular_functioncatalase activity
A0004601molecular_functionperoxidase activity
A0005737cellular_componentcytoplasm
A0006979biological_processresponse to oxidative stress
A0020037molecular_functionheme binding
A0042744biological_processhydrogen peroxide catabolic process
A0046872molecular_functionmetal ion binding
A0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 485
ChainResidue
AARG182
AHIS192
AARG216
AHOH825

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 486
ChainResidue
APHE419
AARG423
AHOH844

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 487
ChainResidue
ASER430
AARG436

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 488
ChainResidue
AARG182
AASN223

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 489
ChainResidue
APRO283
AHIS284
AALA285

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 490
ChainResidue
AARG216
AGLN218

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 491
ChainResidue
AARG45
AARG45
AARG342
AARG342
ATYR343
ATYR343
AHOH657
AHOH657

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE O A 500
ChainResidue
AOMT53
AHIS54
APHE140
AHEM501

site_idAC9
Number of Residues22
DetailsBINDING SITE FOR RESIDUE HEM A 501
ChainResidue
AASP44
AARG51
AOMT53
AHIS54
AARG91
AVAL125
AGLY126
AASN127
APHE140
AGLY195
ASER196
APHE313
AMET329
AARG333
ASER336
ATYR337
AHIS341
AARG344
AO500
AHOH503
AHOH644
AHOH647

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 502
ChainResidue
AGLU38
AHIS42
AARG342
AHIS349
AHOH684

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

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PDB entries from 2024-07-17

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