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2Q2O

Crystal structure of H183C Bacillus subtilis ferrochelatase in complex with deuteroporphyrin IX 2,4-disulfonic acid dihydrochloride

Functional Information from GO Data
ChainGOidnamespacecontents
A0004325molecular_functionferrochelatase activity
A0005737cellular_componentcytoplasm
A0006783biological_processheme biosynthetic process
A0016829molecular_functionlyase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 1000
ChainResidue
AHOH9002
AHOH9003
AHOH9004
AHOH9005
AHOH9006
AHOH9007

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE H01 A 9001
ChainResidue
AARG30
AARG31
AARG33
APHE120
ACYS183
ASER184
ALEU185
AGLN199
AGLY224
AASN225
ATHR226
APRO227
ATRP230
AHOH9026
AHOH9031
AHOH9092
ATYR13
ATYR26
AILE29

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:10704318, ECO:0007744|PDB:1C1H
ChainResidueDetails
ATYR13
AARG31
ACYS183
ALYS188

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:17198378, ECO:0000305|PubMed:21052751
ChainResidueDetails
AGLU20

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00323
ChainResidueDetails
AARG30
ASER54
ATYR125

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:12761666
ChainResidueDetails
AARG46
AASP268
AGLU272

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00323, ECO:0000305|PubMed:12761666, ECO:0000305|PubMed:16140324, ECO:0000305|PubMed:17198378, ECO:0000305|PubMed:21052751
ChainResidueDetails
AGLU264

222926

PDB entries from 2024-07-24

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