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3WNU

The crystal structure of catalase-peroxidase, KatG, from Synechococcus PCC7942

Functional Information from GO Data
ChainGOidnamespacecontents
A0004096molecular_functioncatalase activity
A0004601molecular_functionperoxidase activity
A0005829cellular_componentcytosol
A0006979biological_processresponse to oxidative stress
A0020037molecular_functionheme binding
A0042744biological_processhydrogen peroxide catabolic process
A0046872molecular_functionmetal ion binding
A0070301biological_processcellular response to hydrogen peroxide
A0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE HEB A 801
ChainResidue
AGLY87
AHIS263
AGLY266
ALYS267
ACYS268
AHIS269
ATHR307
ASER308
ATRP314
ATRP406
AHOH915
ALEU88
AHOH943
AHOH978
AILE90
AARG91
ATRP94
APHE245
ALEU258
ATHR259
AGLY262

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 802
ChainResidue
AGLY105
AARG106
AGLY107
ASER476
AHOH1078
AHOH1325

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 803
ChainResidue
ATHR264
ATHR315
AHIS317
AGLN320
AASP322

Functional Information from PROSITE/UniProt
site_idPS00436
Number of Residues12
DetailsPEROXIDASE_2 Peroxidases active site signature. GGlmIRLtWHAA
ChainResidueDetails
AGLY86-ALA97

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AHIS95

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: axial binding residue
ChainResidueDetails
AHIS263

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_01961
ChainResidueDetails
AARG91

site_idSWS_FT_FI4
Number of Residues1
DetailsCROSSLNK: Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-248)
ChainResidueDetails
ATRP94

site_idSWS_FT_FI5
Number of Residues2
DetailsCROSSLNK: Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-94)
ChainResidueDetails
ATYR222
AMET248

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PDB entries from 2024-05-01

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