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3VLJ

Crystal Structure Analysis of the Cyanide Arg409Leu Variant Complexes with o-Dianisidine in KatG from HALOARCULA MARISMORTUI

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
B0004096molecular_functioncatalase activity
B0004601molecular_functionperoxidase activity
B0005829cellular_componentcytosol
B0006979biological_processresponse to oxidative stress
B0020037molecular_functionheme binding
B0042744biological_processhydrogen peroxide catabolic process
B0046872molecular_functionmetal ion binding
B0070301biological_processcellular response to hydrogen peroxide
B0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEM A 800
ChainResidue
APRO88
AVAL264
AHIS265
ATHR304
ASER305
ATRP311
ALEU369
ATHR371
APHE399
ATRP403
ADDJ801
ATRP95
ACYN802
AHOH902
AHOH904
AHOH907
ALEU254
AILE255
AGLY258
AHIS259
APHE261
AGLY262
ALYS263

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE DDJ A 801
ChainResidue
AARG92
APRO124
AASP125
AGLU194
APRO221
APRO270
AGLU271
ASER305
AHEM800

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CYN A 802
ChainResidue
AARG92
ATRP95
AHIS96
AHEM800

site_idAC4
Number of Residues22
DetailsBINDING SITE FOR RESIDUE HEM B 800
ChainResidue
BPRO88
BTRP95
BLEU254
BILE255
BGLY258
BHIS259
BPHE261
BGLY262
BLYS263
BVAL264
BHIS265
BTHR304
BSER305
BTRP311
BTHR371
BPHE399
BTRP403
BDDJ801
BCYN802
BHOH907
BHOH908
BHOH943

site_idAC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE DDJ B 801
ChainResidue
BARG92
BHIS96
BPRO124
BASP125
BGLU194
BPRO221
BPRO270
BTHR304
BSER305
BHEM800
BHOH912

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CYN B 802
ChainResidue
BARG92
BTRP95
BHIS96
BHEM800
BHOH912

Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. TAALIAGGHTF
ChainResidueDetails
ATHR251-PHE261

site_idPS00436
Number of Residues12
DetailsPEROXIDASE_2 Peroxidases active site signature. GPlfIRMaWHSA
ChainResidueDetails
AGLY87-ALA98

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AHIS96
BHIS96

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: axial binding residue
ChainResidueDetails
AHIS259
BHIS259

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Transition state stabilizer
ChainResidueDetails
AARG92
BARG92

site_idSWS_FT_FI4
Number of Residues2
DetailsCROSSLNK: Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-244)
ChainResidueDetails
ATRP95
BTRP95

site_idSWS_FT_FI5
Number of Residues4
DetailsCROSSLNK: Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-95)
ChainResidueDetails
ATYR218
AMET244
BTYR218
BMET244

221051

PDB entries from 2024-06-12

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