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1CK6

BINDING MODE OF SALICYLHYDROXAMIC ACID TO ARTHROMYCES RAMOSUS PEROXIDASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000302biological_processresponse to reactive oxygen species
A0004601molecular_functionperoxidase activity
A0005576cellular_componentextracellular region
A0006979biological_processresponse to oxidative stress
A0020037molecular_functionheme binding
A0034599biological_processcellular response to oxidative stress
A0042744biological_processhydrogen peroxide catabolic process
A0046872molecular_functionmetal ion binding
A0098869biological_processcellular oxidant detoxification
A0140825molecular_functionlactoperoxidase activity
Functional Information from PDB Data
site_idCA1
Number of Residues7
DetailsCALCIUM ION BINDING SITE.
ChainResidue
ACA346
AASP57
AGLY75
AASP77
ASER79
AHOH424
AHOH425

site_idCA2
Number of Residues6
DetailsCALCIUM ION BINDING SITE.
ChainResidue
AASP202
ATHR204
AVAL207
AASP209
ACA347
ASER185

site_idGL1
Number of Residues3
DetailsSUGAR BINDING SITE.
ChainResidue
BNAG1
BNAG2
AASN143

site_idMA1
Number of Residues2
DetailsSUGAR BINDING SITE.
ChainResidue
ABMA350
ASER339

Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. EVVDLLAAHSL
ChainResidueDetails
AGLU176-LEU186

site_idPS00436
Number of Residues12
DetailsPEROXIDASE_2 Peroxidases active site signature. VRkiLRIvFHDA
ChainResidueDetails
AVAL47-ALA58

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AHIS56

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING:
ChainResidueDetails
AASP57
AGLY75
AASP77
ASER79
ASER185
AASP202
ATHR204
AVAL207
AASP209

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: axial binding residue
ChainResidueDetails
AHIS184

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Transition state stabilizer
ChainResidueDetails
AARG52

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:8289254
ChainResidueDetails
AGLN1

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000269|PubMed:1576150
ChainResidueDetails
AASN143

226707

PDB entries from 2024-10-30

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