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6IED

Crystal structure of heme A synthase from Bacillus subtilis

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0006783biological_processheme biosynthetic process
A0006784biological_processheme A biosynthetic process
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016653molecular_functionoxidoreductase activity, acting on NAD(P)H, heme protein as acceptor
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue HEM A 601
ChainResidue
AARG37
AILE255
AGLN258
AGLY262
ALEU270
AHIS278
AVAL176
AGLY179
AALA180
AARG183
ASER188
AHIS216
AARG217
AALA220

site_idAC2
Number of Residues4
Detailsbinding site for residue CU A 602
ChainResidue
AMET-4
AGLU-2
AASP145
AHIS209

site_idAC3
Number of Residues5
Detailsbinding site for residue SO4 A 603
ChainResidue
ATHR27
ALYS28
ATHR29
AARG183
AHIS184

site_idAC4
Number of Residues6
Detailsbinding site for residue SO4 A 604
ChainResidue
AGLY158
ALYS159
ALYS160
AMET161
AHIS233
ATYR238

site_idAC5
Number of Residues8
Detailsbinding site for residue OLC A 605
ChainResidue
AARG87
AGLU88
APHE91
ALEU92
AMET95
AILE170
ACYS290
ALEU294

site_idAC6
Number of Residues5
Detailsbinding site for residue OLC A 606
ChainResidue
ALEU139
APHE142
AGLU143
ALYS146
ATHR150

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues34
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:30397130
ChainResidueDetails
AMET1-ASN2
ATRP79-GLU88
ALEU140-LYS159
ASER237-LYS242

site_idSWS_FT_FI2
Number of Residues22
DetailsTRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:30397130, ECO:0007744|PDB:6A2J, ECO:0007744|PDB:6IED
ChainResidueDetails
ALYS3-LEU25

site_idSWS_FT_FI3
Number of Residues52
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:30397130
ChainResidueDetails
AVAL26-ASN51
AGLY114-SER115
AGLU186-GLU210
AGLU269-ALA271

site_idSWS_FT_FI4
Number of Residues26
DetailsTRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:30397130, ECO:0007744|PDB:6A2J, ECO:0007744|PDB:6IED
ChainResidueDetails
APRO52-SER78

site_idSWS_FT_FI5
Number of Residues24
DetailsTRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:30397130, ECO:0007744|PDB:6A2J, ECO:0007744|PDB:6IED
ChainResidueDetails
ATHR89-PHE113

site_idSWS_FT_FI6
Number of Residues23
DetailsTRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:30397130, ECO:0007744|PDB:6A2J, ECO:0007744|PDB:6IED
ChainResidueDetails
AASN116-LEU139

site_idSWS_FT_FI7
Number of Residues25
DetailsTRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:30397130, ECO:0007744|PDB:6A2J, ECO:0007744|PDB:6IED
ChainResidueDetails
ALYS160-THR185

site_idSWS_FT_FI8
Number of Residues25
DetailsTRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:30397130, ECO:0007744|PDB:6A2J, ECO:0007744|PDB:6IED
ChainResidueDetails
ATRP211-THR236

site_idSWS_FT_FI9
Number of Residues25
DetailsTRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:30397130, ECO:0007744|PDB:6A2J, ECO:0007744|PDB:6IED
ChainResidueDetails
AGLN243-SER268

site_idSWS_FT_FI10
Number of Residues22
DetailsTRANSMEM: Helical; Name=8 => ECO:0000269|PubMed:30397130, ECO:0007744|PDB:6A2J, ECO:0007744|PDB:6IED
ChainResidueDetails
ALEU272-LEU294

site_idSWS_FT_FI11
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01664, ECO:0000305|PubMed:30397130
ChainResidueDetails
AGLU57

site_idSWS_FT_FI12
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000255|HAMAP-Rule:MF_01664, ECO:0000305|PubMed:30397130
ChainResidueDetails
AHIS60
AHIS123

site_idSWS_FT_FI13
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000255|HAMAP-Rule:MF_01664, ECO:0000269|PubMed:30397130, ECO:0007744|PDB:6A2J, ECO:0007744|PDB:6IED
ChainResidueDetails
AHIS216
AHIS278

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PDB entries from 2024-07-17

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