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1OLT

Coproporphyrinogen III oxidase (HemN) from Escherichia coli is a Radical SAM enzyme.

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004109molecular_functioncoproporphyrinogen oxidase activity
A0005737cellular_componentcytoplasm
A0006779biological_processporphyrin-containing compound biosynthetic process
A0006782biological_processprotoporphyrinogen IX biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0019353biological_processprotoporphyrinogen IX biosynthetic process from glutamate
A0046872molecular_functionmetal ion binding
A0051536molecular_functioniron-sulfur cluster binding
A0051539molecular_function4 iron, 4 sulfur cluster binding
A0051989molecular_functioncoproporphyrinogen dehydrogenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE SAM A 501
ChainResidue
APHE68
AASP147
AGLY170
AGLN172
AARG184
AASP209
AILE211
APHE240
AASN241
ATYR242
AALA243
ACYS69
AGLN252
ASF4500
ASAM502
AHOH2179
AGLY70
ACYS71
AGLY112
AGLY113
ATHR114
AGLU145
AVAL146

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE SAM A 502
ChainResidue
ATYR56
AHIS58
AGLY111
AGLY112
AGLU145
APHE240
APHE310
AGLN311
ASER327
AALA328
AILE329
ASAM501
AHOH2342
AHOH2391
AHOH2392
AHOH2393
AHOH2394
AHOH2396

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SF4 A 500
ChainResidue
ACYS62
ACYS66
APHE68
ACYS69
ALYS73
AGLY113
ATHR114
AARG149
AARG184
ASAM501

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues233
DetailsDomain: {"description":"Radical SAM core","evidences":[{"source":"PROSITE-ProRule","id":"PRU01266","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"14633981","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1OLT","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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