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2C8J

CRYSTAL STRUCTURE OF ferrochelatase HemH-1 from Bacillus anthracis, str. Ames

Functional Information from GO Data
ChainGOidnamespacecontents
A0004325molecular_functionferrochelatase activity
A0005737cellular_componentcytoplasm
A0006779biological_processporphyrin-containing compound biosynthetic process
A0006783biological_processheme biosynthetic process
A0016829molecular_functionlyase activity
A0046872molecular_functionmetal ion binding
B0004325molecular_functionferrochelatase activity
B0005737cellular_componentcytoplasm
B0006779biological_processporphyrin-containing compound biosynthetic process
B0006783biological_processheme biosynthetic process
B0016829molecular_functionlyase activity
B0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00534
Number of Residues19
DetailsFERROCHELATASE Ferrochelatase signature. LIvSaHSLPekii.AmGDp...Y
ChainResidueDetails
ALEU177-TYR195

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000255|HAMAP-Rule:MF_00323
ChainResidueDetails
ATYR12
BTYR12

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00323
ChainResidueDetails
AARG29
BTYR124
BHIS182
BGLU263
AARG45
ASER53
ATYR124
AHIS182
AGLU263
BARG29
BARG45
BSER53

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1hrk
ChainResidueDetails
AHIS182
AGLU263
AHIS261

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1hrk
ChainResidueDetails
BHIS182
BGLU263
BHIS261

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PDB entries from 2025-06-18

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