4L9Y
Crystal Structure of Rhodobacter sphaeroides malyl-CoA lyase in complex with magnesium, glyoxylate, and propionyl-CoA
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0003824 | molecular_function | catalytic activity |
A | 0006107 | biological_process | oxaloacetate metabolic process |
A | 0016829 | molecular_function | lyase activity |
A | 0043959 | molecular_function | L-erythro-3-methylmalyl-CoA lyase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0047777 | molecular_function | (S)-citramalyl-CoA lyase activity |
A | 0050083 | molecular_function | malyl-CoA lyase activity |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0006107 | biological_process | oxaloacetate metabolic process |
B | 0016829 | molecular_function | lyase activity |
B | 0043959 | molecular_function | L-erythro-3-methylmalyl-CoA lyase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0047777 | molecular_function | (S)-citramalyl-CoA lyase activity |
B | 0050083 | molecular_function | malyl-CoA lyase activity |
C | 0000287 | molecular_function | magnesium ion binding |
C | 0003824 | molecular_function | catalytic activity |
C | 0006107 | biological_process | oxaloacetate metabolic process |
C | 0016829 | molecular_function | lyase activity |
C | 0043959 | molecular_function | L-erythro-3-methylmalyl-CoA lyase activity |
C | 0046872 | molecular_function | metal ion binding |
C | 0047777 | molecular_function | (S)-citramalyl-CoA lyase activity |
C | 0050083 | molecular_function | malyl-CoA lyase activity |
D | 0000287 | molecular_function | magnesium ion binding |
D | 0003824 | molecular_function | catalytic activity |
D | 0006107 | biological_process | oxaloacetate metabolic process |
D | 0016829 | molecular_function | lyase activity |
D | 0043959 | molecular_function | L-erythro-3-methylmalyl-CoA lyase activity |
D | 0046872 | molecular_function | metal ion binding |
D | 0047777 | molecular_function | (S)-citramalyl-CoA lyase activity |
D | 0050083 | molecular_function | malyl-CoA lyase activity |
E | 0000287 | molecular_function | magnesium ion binding |
E | 0003824 | molecular_function | catalytic activity |
E | 0006107 | biological_process | oxaloacetate metabolic process |
E | 0016829 | molecular_function | lyase activity |
E | 0043959 | molecular_function | L-erythro-3-methylmalyl-CoA lyase activity |
E | 0046872 | molecular_function | metal ion binding |
E | 0047777 | molecular_function | (S)-citramalyl-CoA lyase activity |
E | 0050083 | molecular_function | malyl-CoA lyase activity |
F | 0000287 | molecular_function | magnesium ion binding |
F | 0003824 | molecular_function | catalytic activity |
F | 0006107 | biological_process | oxaloacetate metabolic process |
F | 0016829 | molecular_function | lyase activity |
F | 0043959 | molecular_function | L-erythro-3-methylmalyl-CoA lyase activity |
F | 0046872 | molecular_function | metal ion binding |
F | 0047777 | molecular_function | (S)-citramalyl-CoA lyase activity |
F | 0050083 | molecular_function | malyl-CoA lyase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 401 |
Chain | Residue |
A | GLU141 |
A | ASP168 |
A | HOH501 |
A | HOH519 |
A | HOH546 |
A | HOH602 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL A 402 |
Chain | Residue |
A | ASP168 |
A | HOH501 |
A | GLY165 |
A | ALA166 |
A | ALA167 |
site_id | AC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE 1VU B 401 |
Chain | Residue |
A | ASP299 |
B | PHE19 |
B | GLY20 |
B | ARG24 |
B | LYS30 |
B | MET31 |
B | ARG76 |
B | ALA167 |
B | ILE180 |
B | ILE251 |
B | HIS252 |
B | PRO253 |
B | GLV402 |
B | HOH510 |
B | HOH661 |
B | HOH691 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GLV B 402 |
Chain | Residue |
B | ARG76 |
B | GLU141 |
B | GLY165 |
B | ALA166 |
B | ALA167 |
B | ASP168 |
B | PRO223 |
B | 1VU401 |
B | MG403 |
B | HOH510 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 403 |
Chain | Residue |
B | ASP45 |
B | GLU141 |
B | ASP168 |
B | GLV402 |
B | HOH510 |
B | HOH724 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG C 401 |
Chain | Residue |
C | ASP45 |
C | GLU141 |
C | ASP168 |
C | HOH502 |
C | HOH503 |
C | HOH507 |
C | HOH763 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CL C 402 |
Chain | Residue |
C | GLY165 |
C | ALA166 |
C | ALA167 |
C | ASP168 |
C | HOH502 |
C | HOH627 |
site_id | AC8 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GLV D 401 |
Chain | Residue |
D | ARG76 |
D | GLU141 |
D | GLY165 |
D | ALA166 |
D | ALA167 |
D | ASP168 |
D | PRO223 |
D | TRP249 |
D | MG402 |
D | HOH501 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG D 402 |
Chain | Residue |
D | GLU141 |
D | ASP168 |
D | GLV401 |
D | HOH501 |
D | HOH733 |
site_id | BC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG E 401 |
Chain | Residue |
E | ASP45 |
E | GLU141 |
E | ASP168 |
E | HOH501 |
E | HOH513 |
E | HOH724 |
E | HOH757 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CL E 402 |
Chain | Residue |
E | GLY165 |
E | ALA166 |
E | ALA167 |
E | ASP168 |
E | PRO223 |
E | HOH724 |
site_id | BC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG F 401 |
Chain | Residue |
F | ASP45 |
F | GLU141 |
F | ASP168 |
F | HOH503 |
F | HOH506 |
F | HOH526 |
F | HOH747 |
site_id | BC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CL F 402 |
Chain | Residue |
F | GLY165 |
F | ALA166 |
F | ALA167 |
F | ASP168 |
F | PRO223 |
F | HOH747 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:24206647, ECO:0007744|PDB:4L9Y |
Chain | Residue | Details |
A | PHE19 | |
E | ARG24 | |
F | PHE19 | |
F | ARG24 | |
A | ARG24 | |
B | PHE19 | |
B | ARG24 | |
C | PHE19 | |
C | ARG24 | |
D | PHE19 | |
D | ARG24 | |
E | PHE19 |
site_id | SWS_FT_FI2 |
Number of Residues | 18 |
Details | BINDING: BINDING => ECO:0000269|PubMed:24206647, ECO:0007744|PDB:4L9Z |
Chain | Residue | Details |
A | LYS30 | |
D | LYS30 | |
D | ALA167 | |
D | ILE251 | |
E | LYS30 | |
E | ALA167 | |
E | ILE251 | |
F | LYS30 | |
F | ALA167 | |
F | ILE251 | |
A | ALA167 | |
A | ILE251 | |
B | LYS30 | |
B | ALA167 | |
B | ILE251 | |
C | LYS30 | |
C | ALA167 | |
C | ILE251 |
site_id | SWS_FT_FI3 |
Number of Residues | 18 |
Details | BINDING: BINDING => ECO:0000269|PubMed:24206647, ECO:0007744|PDB:4L9Y, ECO:0007744|PDB:4L9Z |
Chain | Residue | Details |
A | ARG76 | |
D | ARG76 | |
D | GLU141 | |
D | ASP168 | |
E | ARG76 | |
E | GLU141 | |
E | ASP168 | |
F | ARG76 | |
F | GLU141 | |
F | ASP168 | |
A | GLU141 | |
A | ASP168 | |
B | ARG76 | |
B | GLU141 | |
B | ASP168 | |
C | ARG76 | |
C | GLU141 | |
C | ASP168 |