Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3VLL

Crystal Structure Analysis of the Ser305Ala variant of KatG from HALOARCULA MARISMORTUI Complexes with Inhibitor SHA

Functional Information from GO Data
ChainGOidnamespacecontents
A0004096molecular_functioncatalase activity
A0004601molecular_functionperoxidase activity
A0005829cellular_componentcytosol
A0006979biological_processresponse to oxidative stress
A0016491molecular_functionoxidoreductase activity
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
B0016491molecular_functionoxidoreductase activity
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 Residues18
DetailsBINDING SITE FOR RESIDUE HEM A 800
ChainResidue
APRO88
ALYS263
AVAL264
AHIS265
ATRP311
ATHR371
ATRP403
AHOH922
AHOH938
AHOH968
AILE91
ATRP95
APHE241
ALEU254
AILE255
AGLY258
AHIS259
AGLY262

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SHA A 801
ChainResidue
ATRP95
AHIS96
AASP125
ALEU216
AILE217
APRO221

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE HEM B 800
ChainResidue
BPRO88
BILE91
BTRP95
BVAL219
BLEU254
BILE255
BGLY258
BHIS259
BGLY262
BLYS263
BHIS265
BTHR304
BALA305
BTRP311
BLEU369
BTHR371
BPHE399
BSHA801
BHOH925
BHOH975
BHOH981

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SHA B 801
ChainResidue
BARG92
BTRP95
BHIS96
BASP125
BVAL219
BHEM800

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

237423

PDB entries from 2025-06-11

PDB statisticsPDBj update infoContact PDBjnumon