4L9Z
Crystal Structure of Rhodobacter sphaeroides malyl-CoA lyase in complex with magnesium, oxalate, and 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 | 19 |
Details | BINDING SITE FOR RESIDUE COA A 401 |
Chain | Residue |
A | PHE19 |
A | HIS252 |
A | PRO253 |
A | OXL402 |
A | HOH513 |
A | HOH743 |
A | HOH799 |
A | HOH809 |
A | HOH844 |
A | HOH873 |
C | ASP299 |
A | GLY20 |
A | PRO21 |
A | LEU27 |
A | LYS30 |
A | MET31 |
A | SER46 |
A | ARG76 |
A | ILE251 |
site_id | AC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE OXL A 402 |
Chain | Residue |
A | ARG76 |
A | GLU141 |
A | GLY165 |
A | ALA166 |
A | ALA167 |
A | ASP168 |
A | PRO223 |
A | TRP249 |
A | COA401 |
A | MG403 |
A | HOH505 |
A | HOH513 |
C | HOH609 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 403 |
Chain | Residue |
A | GLU141 |
A | ASP168 |
A | OXL402 |
A | HOH502 |
A | HOH505 |
site_id | AC4 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE COA B 401 |
Chain | Residue |
A | ASP299 |
B | PHE19 |
B | GLY20 |
B | PRO21 |
B | ARG24 |
B | LEU27 |
B | LYS30 |
B | MET31 |
B | ASP42 |
B | SER46 |
B | ARG76 |
B | TRP249 |
B | ILE251 |
B | HIS252 |
B | PRO253 |
B | OXL402 |
B | HOH523 |
B | HOH650 |
B | HOH743 |
B | HOH886 |
B | HOH911 |
site_id | AC5 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE OXL B 402 |
Chain | Residue |
B | ARG76 |
B | GLU141 |
B | GLY165 |
B | ALA166 |
B | ALA167 |
B | ASP168 |
B | PRO223 |
B | TRP249 |
B | COA401 |
B | MG403 |
B | HOH504 |
B | HOH523 |
B | HOH894 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 403 |
Chain | Residue |
B | GLU141 |
B | ASP168 |
B | OXL402 |
B | HOH502 |
B | HOH504 |
site_id | AC7 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE COA C 401 |
Chain | Residue |
B | ASP299 |
C | PHE19 |
C | GLY20 |
C | PRO21 |
C | ARG24 |
C | LYS30 |
C | MET31 |
C | SER46 |
C | ARG76 |
C | ILE251 |
C | HIS252 |
C | PRO253 |
C | OXL402 |
C | HOH528 |
C | HOH587 |
C | HOH678 |
C | HOH811 |
C | HOH844 |
site_id | AC8 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE OXL C 402 |
Chain | Residue |
C | ASP168 |
C | PRO223 |
C | COA401 |
C | MG403 |
C | HOH528 |
C | HOH714 |
C | HOH931 |
C | ARG76 |
C | GLU141 |
C | GLY165 |
C | ALA166 |
C | ALA167 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG C 403 |
Chain | Residue |
C | GLU141 |
C | ASP168 |
C | OXL402 |
C | HOH504 |
C | HOH931 |
site_id | BC1 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE COA D 401 |
Chain | Residue |
D | PHE19 |
D | GLY20 |
D | PRO21 |
D | ARG24 |
D | LEU27 |
D | LYS30 |
D | MET31 |
D | SER46 |
D | ARG76 |
D | ILE251 |
D | HIS252 |
D | PRO253 |
D | OXL402 |
D | HOH517 |
D | HOH771 |
D | HOH864 |
D | HOH904 |
D | HOH905 |
F | VAL292 |
F | ASP299 |
site_id | BC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE OXL D 402 |
Chain | Residue |
D | ARG76 |
D | GLU141 |
D | GLY165 |
D | ALA166 |
D | ALA167 |
D | ASP168 |
D | PRO223 |
D | TRP249 |
D | COA401 |
D | MG403 |
D | HOH506 |
D | HOH517 |
F | HOH753 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG D 403 |
Chain | Residue |
D | GLU141 |
D | ASP168 |
D | OXL402 |
D | HOH506 |
D | HOH507 |
site_id | BC4 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE COA E 401 |
Chain | Residue |
D | ASP299 |
E | PHE19 |
E | GLY20 |
E | PRO21 |
E | ARG24 |
E | LEU27 |
E | LYS30 |
E | MET31 |
E | ASP42 |
E | SER46 |
E | ARG76 |
E | ILE251 |
E | HIS252 |
E | PRO253 |
E | OXL402 |
E | HOH549 |
E | HOH556 |
E | HOH592 |
E | HOH895 |
site_id | BC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE OXL E 402 |
Chain | Residue |
E | ARG76 |
E | GLU141 |
E | GLY165 |
E | ALA166 |
E | ALA167 |
E | ASP168 |
E | PRO223 |
E | TRP249 |
E | COA401 |
E | MG403 |
E | HOH503 |
E | HOH505 |
E | HOH549 |
E | HOH691 |
site_id | BC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG E 403 |
Chain | Residue |
E | GLU141 |
E | ASP168 |
E | OXL402 |
E | HOH503 |
E | HOH505 |
site_id | BC7 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE COA F 401 |
Chain | Residue |
E | ASP299 |
F | PHE19 |
F | GLY20 |
F | PRO21 |
F | ARG24 |
F | LEU27 |
F | MET31 |
F | SER46 |
F | ARG76 |
F | ILE251 |
F | HIS252 |
F | PRO253 |
F | OXL402 |
F | HOH524 |
F | HOH873 |
F | HOH900 |
site_id | BC8 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE OXL F 402 |
Chain | Residue |
F | ARG76 |
F | GLU141 |
F | GLY165 |
F | ALA166 |
F | ALA167 |
F | ASP168 |
F | PRO223 |
F | TRP249 |
F | COA401 |
F | MG403 |
F | HOH507 |
F | HOH524 |
F | HOH637 |
site_id | BC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG F 403 |
Chain | Residue |
F | GLU141 |
F | ASP168 |
F | OXL402 |
F | HOH504 |
F | HOH507 |
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 |