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6BMT

Crystal Structure of a Recombinant form of Human Myeloperoxidase Bound to an Inhibitor from Staphylococcus delphini

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0006979biological_processresponse to oxidative stress
A0020037molecular_functionheme binding
Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. EMPELTSMHTL
ChainResidueDetails
AGLU408-LEU418

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AHIS261

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: covalent => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX
ChainResidueDetails
AASP260
AGLU408
AMET409

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING:
ChainResidueDetails
AASP262

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:10766826, ECO:0000269|PubMed:11705390, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:1D2V, ECO:0007744|PDB:1D7W, ECO:0007744|PDB:1DNU, ECO:0007744|PDB:1DNW, ECO:0007744|PDB:1MHL
ChainResidueDetails
APHE336
AASP338
ASER340
ATHR334

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX
ChainResidueDetails
AHIS502

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Transition state stabilizer
ChainResidueDetails
AARG405

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:7840679
ChainResidueDetails
ACYS316

site_idSWS_FT_FI8
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952
ChainResidueDetails
AASN139

site_idSWS_FT_FI9
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:20332087
ChainResidueDetails
AASN323

site_idSWS_FT_FI10
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20332087, ECO:0000269|PubMed:23843990, ECO:0007744|PDB:4EJX
ChainResidueDetails
AASN391
AASN355

site_idSWS_FT_FI11
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:20332087, ECO:0000269|PubMed:23843990, ECO:0007744|PDB:4EJX
ChainResidueDetails
AASN483

site_idSWS_FT_FI12
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20332087
ChainResidueDetails
AASN729

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 601
ChainResidueDetails
AHIS261proton shuttle (general acid/base)
AARG405electrostatic stabiliser

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PDB entries from 2024-06-12

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