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6S07

Structure of formylglycine-generating enzyme at 1.04 A in complex with copper and substrate reveals an acidic pocket for binding and acti-vation of molecular oxygen.

Functional Information from GO Data
ChainGOidnamespacecontents
A0016491molecular_functionoxidoreductase activity
A0018158biological_processprotein oxidation
A0043687biological_processpost-translational protein modification
A0046872molecular_functionmetal ion binding
A0120147molecular_functionformylglycine-generating oxidase activity
A1903136molecular_functioncuprous ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue CU1 A 401
ChainResidue
ACYS269
ACYS274
CCYS7

site_idAC2
Number of Residues6
Detailsbinding site for residue CA A 402
ChainResidue
AASN222
AVAL223
AGLY225
AVAL227
AGLU229
AGLY265

site_idAC3
Number of Residues6
Detailsbinding site for residue CA A 403
ChainResidue
AASN188
AILE189
AASP202
ATYR204
AHOH532
AHOH539

site_idAC4
Number of Residues3
Detailsbinding site for residue CL A 404
ChainResidue
APRO131
AASN132
AHIS133

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:28544744, ECO:0007744|PDB:5NXL, ECO:0007744|PDB:5NYY
ChainResidueDetails
AASN188
AILE189
AASP202
ATYR204
AASN222
AVAL223
AGLY225
AVAL227

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:27862795, ECO:0000269|PubMed:28544744, ECO:0007744|PDB:5NXL, ECO:0007744|PDB:5NYY
ChainResidueDetails
ACYS269
ACYS274

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PDB entries from 2024-09-04

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