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1UB2

Crystal structure of catalase-peroxidase from Synechococcus PCC 7942

Functional Information from GO Data
ChainGOidnamespacecontents
A0004096molecular_functioncatalase activity
A0004601molecular_functionperoxidase activity
A0006979biological_processresponse to oxidative stress
A0020037molecular_functionheme binding
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEM A 721
ChainResidue
AGLY86
AHIS262
AGLY265
ALYS266
ACYS267
AHIS268
ATHR306
ASER307
ATRP313
AALA374
APHE402
ALEU87
ATRP406
AHOH742
AHOH743
AHOH769
AILE89
AARG90
ATRP93
APRO224
ALEU257
ATHR258
AGLY261

Functional Information from PROSITE/UniProt
site_idPS00436
Number of Residues12
DetailsPEROXIDASE_2 Peroxidases active site signature. GGlmIRLtWHAA
ChainResidueDetails
AGLY85-ALA96

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AALA95

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: axial binding residue
ChainResidueDetails
ATHR263

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_01961
ChainResidueDetails
ALEU91

site_idSWS_FT_FI4
Number of Residues1
DetailsCROSSLNK: Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-248)
ChainResidueDetails
AHIS94

site_idSWS_FT_FI5
Number of Residues2
DetailsCROSSLNK: Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-94)
ChainResidueDetails
AVAL222
AALA248

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1apx
ChainResidueDetails
AARG90
AASP123
AHIS94

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1apx
ChainResidueDetails
AARG90
AASN124
AHIS94

237423

PDB entries from 2025-06-11

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