Structure of PDB 2bwo Chain D Binding Site BS01

Receptor Information
>2bwo Chain D (length=397) Species: 1061 (Rhodobacter capsulatus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MDYNLALDKAIQKLHDEGRYRTFIDIEREKGAFPKAQWNRPDGGKQDITV
WCGNDYLGMGQHPVVLAAMHEALEAVGAGSGGTRNISGTTAYHRRLEAEI
AGLHQKEAALVFSSAYNANDATLSTLRVLFPGLIIYSDSLNHASMIEGIK
RNAGPKRIFRHNDVAHLRELIAADDPAAPKLIAFESVYSMDGDFGPIKEI
CDIAEEFGALTYIDEVHAVGMYGPRGAGVAERDGLMHRIDIFNGTLAKAY
GVFGGYIAASARMVDAVRSYAPGFIFSTSLPPAIAAGAQASIAFLKTAEG
QKLRDAQQMHAKVLKMRLKALGMPIIDHGSHIVPVVIGDPVHTKAVSDML
LSDYGVYVQPINFPTVPRGTERLRFTPSPVHDLKQIDGLVHAMDLLW
Ligand information
Ligand IDSCA
InChIInChI=1S/C25H40N7O19P3S/c1-25(2,20(38)23(39)28-6-5-14(33)27-7-8-55-16(36)4-3-15(34)35)10-48-54(45,46)51-53(43,44)47-9-13-19(50-52(40,41)42)18(37)24(49-13)32-12-31-17-21(26)29-11-30-22(17)32/h11-13,18-20,24,37-38H,3-10H2,1-2H3,(H,27,33)(H,28,39)(H,34,35)(H,43,44)(H,45,46)(H2,26,29,30)(H2,40,41,42)/t13-,18-,19-,20+,24-/m1/s1
InChIKeyVNOYUJKHFWYWIR-ITIYDSSPSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=C(O)CCC(=O)SCCNC(=O)CCNC(=O)C(O)C(C)(C)COP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3OP(=O)(O)O
OpenEye OEToolkits 1.5.0CC(C)(COP(=O)(O)OP(=O)(O)OCC1C(C(C(O1)n2cnc3c2ncnc3N)O)OP(=O)(O)O)C(C(=O)NCCC(=O)NCCSC(=O)CCC(=O)O)O
CACTVS 3.341CC(C)(CO[P@](O)(=O)O[P@@](O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O[P](O)(O)=O)n2cnc3c(N)ncnc23)[C@@H](O)C(=O)NCCC(=O)NCCSC(=O)CCC(O)=O
CACTVS 3.341CC(C)(CO[P](O)(=O)O[P](O)(=O)OC[CH]1O[CH]([CH](O)[CH]1O[P](O)(O)=O)n2cnc3c(N)ncnc23)[CH](O)C(=O)NCCC(=O)NCCSC(=O)CCC(O)=O
OpenEye OEToolkits 1.5.0CC(C)(CO[P@@](=O)(O)O[P@](=O)(O)OC[C@@H]1[C@H]([C@H]([C@@H](O1)n2cnc3c2ncnc3N)O)OP(=O)(O)O)[C@H](C(=O)NCCC(=O)NCCSC(=O)CCC(=O)O)O
FormulaC25 H40 N7 O19 P3 S
NameSUCCINYL-COENZYME A
ChEMBL
DrugBankDB03699
ZINCZINC000008551116
PDB chain2bwo Chain D Residue 500 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB2bwo Crystal Structure of 5-Aminolevulinate Synthase, the First Enzyme of Heme Biosynthesis, and its Link to Xlsa in Humans.
Resolution2.8 Å
Binding residue
(original residue number in PDB)		R21 S137 S139 N141 H142 A143 I146 K150 K156 I158 P364 T365
Binding residue
(residue number reindexed from 1)		R21 S137 S139 N141 H142 A143 I146 K150 K156 I158 P364 T365
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) N54 H142 E185 S189 D214 H217 K248
Catalytic site (residue number reindexed from 1) N54 H142 E185 S189 D214 H217 K248
Enzyme Commision number 2.3.1.37: 5-aminolevulinate synthase.
Gene Ontology
Molecular Function
GO:0003870 5-aminolevulinate synthase activity
GO:0016740 transferase activity
GO:0016746 acyltransferase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0006782 protoporphyrinogen IX biosynthetic process
GO:0006783 heme biosynthetic process
GO:0009058 biosynthetic process
GO:0033014 tetrapyrrole biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2bwo, PDBe:2bwo, PDBj:2bwo
PDBsum2bwo
PubMed16121195
UniProtP18079|HEM1_RHOCB 5-aminolevulinate synthase (Gene Name=hemA)

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