Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1CPO

CHLOROPEROXIDASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
Functional Information from PDB Data
site_idHE1
Number of Residues2
DetailsHEME PROXIMAL SITE.
ChainResidue
AHEM396
ACYS29

site_idHEM
Number of Residues5
DetailsHEME DISTAL SITE.
ChainResidue
AHEM396
AGLU183
AHIS105
APHE186
AHOH801

site_idMN
Number of Residues7
DetailsMANGANESE BINDING SITE.
ChainResidue
AGLU104
AHIS105
ASER108
AHOH802
AHOH803
AMN301
AHEM396

site_idNG1
Number of Residues2
DetailsN-GLYCOSYLATION SITE.
ChainResidue
AASN12
ANAG512

site_idNG2
Number of Residues7
DetailsN-GLYCOSYLATION SITE.
ChainResidue
AASN93
BNAG1
BNAG2
BBMA3
BXYS6
BXYS4
BMAN5

site_idNG3
Number of Residues3
DetailsN-GLYCOSYLATION SITE.
ChainResidue
AASN216
CNAG1
CNAG2

site_idOG1
Number of Residues2
DetailsO-GLYCOSYLATION SITE.
ChainResidue
ATHR238
AMAN738

site_idOG2
Number of Residues2
DetailsO-GLYCOSYLATION SITE.
ChainResidue
ASER239
AMAN739

site_idOG3
Number of Residues2
DetailsO-GLYCOSYLATION SITE.
ChainResidue
ASER241
AMAN741

site_idOG4
Number of Residues2
DetailsO-GLYCOSYLATION SITE.
ChainResidue
ASER242
AMAN742

site_idOG5
Number of Residues2
DetailsO-GLYCOSYLATION SITE.
ChainResidue
ASER248
AXYS748

site_idOG6
Number of Residues2
DetailsO-GLYCOSYLATION SITE.
ChainResidue
ATHR250
AMAN750

site_idOG7
Number of Residues2
DetailsO-GLYCOSYLATION SITE.
ChainResidue
ASER251
AMAN751

site_idOG8
Number of Residues2
DetailsO-GLYCOSYLATION SITE.
ChainResidue
ATHR252
AMAN752

site_idOG9
Number of Residues3
DetailsO-GLYCOSYLATION SITE.
ChainResidue
ATHR275
DMAN1
DARB2

site_idOGA
Number of Residues2
DetailsO-GLYCOSYLATION SITE.
ChainResidue
ATHR283
AMAN783

site_idOGB
Number of Residues2
DetailsO-GLYCOSYLATION SITE.
ChainResidue
ATHR293
AMAN793

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE:
ChainResidueDetails
AGLU183

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: axial binding residue
ChainResidueDetails
ACYS29

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING:
ChainResidueDetails
AGLU104
AHIS105
ASER108

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:8747463
ChainResidueDetails
APCA0

site_idSWS_FT_FI5
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine
ChainResidueDetails
AASN12
AASN93
AASN216

site_idSWS_FT_FI6
Number of Residues3
DetailsCARBOHYD: O-linked (Man) threonine
ChainResidueDetails
ATHR238
ATHR250
ATHR252

site_idSWS_FT_FI7
Number of Residues4
DetailsCARBOHYD: O-linked (Man) serine
ChainResidueDetails
ASER239
ASER241
ASER242
ASER251

site_idSWS_FT_FI8
Number of Residues1
DetailsCARBOHYD: O-linked (Man) serine => ECO:0000305
ChainResidueDetails
ASER248

site_idSWS_FT_FI9
Number of Residues3
DetailsCARBOHYD: O-linked (Man...) threonine
ChainResidueDetails
ATHR275
ATHR283
ATHR293

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 250
ChainResidueDetails
ACYS29activator, covalently attached, metal ligand
AHIS105electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AASP106electrostatic stabiliser, hydrogen bond acceptor, increase acidity, increase basicity
AGLU183activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon