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6XTS

Crystal structure reveals non-coordinative binding of O2 to the copper center of the formylglycine-generating enzyme - FGE:Cu:S:O2-1d complex

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 Residues5
Detailsbinding site for residue CU1 A 401
ChainResidue
ACYS269
ACYS274
AARG276
AOXY405
CCYS7

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

site_idAC3
Number of Residues6
Detailsbinding site for residue CA A 403
ChainResidue
AASN188
AILE189
AASP202
ATYR204
AHOH556
AHOH594

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

site_idAC5
Number of Residues6
Detailsbinding site for residue OXY A 405
ChainResidue
ATRP228
ASER266
ACYS269
AHIS293
ACU1401
AHOH510

site_idAC6
Number of Residues7
Detailsbinding site for residue SOA C 101
ChainResidue
AARG248
AILE249
ATYR273
CALA2
CTHR3
CHOH211
CHOH212

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

220113

PDB entries from 2024-05-22

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