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1M85

Structure of Proteus mirabilis catalase for the native form

Replaces:  2CAEReplaces:  1CAE
Functional Information from GO Data
ChainGOidnamespacecontents
A0004096molecular_functioncatalase activity
A0004601molecular_functionperoxidase activity
A0005737cellular_componentcytoplasm
A0006979biological_processresponse to oxidative stress
A0016491molecular_functionoxidoreductase activity
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 Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 485
ChainResidue
AARG182
AHIS192
AARG216
AHOH1405
AHOH1493
AHOH1494

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 486
ChainResidue
AHOH1384
AHOH1399
AHOH1457
AHOH1458
AARG423
AHOH1062
AHOH1384

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 487
ChainResidue
ASER430
AASP432
AARG436

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 488
ChainResidue
AARG182
AASN223
AHOH1270

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 489
ChainResidue
APRO283
AHIS284
AALA285
AHOH1428

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 490
ChainResidue
AARG216
AGLN218
AHOH1359

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 A 491
ChainResidue
AHOH1470

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 492
ChainResidue
AARG45
AARG45
AARG342
AARG342
ATYR343
ATYR343
AHOH1171
AHOH1171

site_idAC9
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEM A 1001
ChainResidue
AASP44
AARG51
AHIS54
AARG91
AVAL125
AGLY126
AASN127
APHE140
AGLY195
ASER196
APHE313
AMET329
AARG333
ASER336
ATYR337
AHIS341
AARG344
AHOH1003
AHOH1152
AHOH1156

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1002
ChainResidue
AGLU38
AHIS42
AARG342
AHIS349
AHOH1103
AHOH1135

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
DetailsActive site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"7791219","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Methionine sulfone","evidences":[{"source":"PubMed","id":"7786407","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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 2025-12-10

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