3RMU
Crystal structure of human Methylmalonyl-CoA epimerase, MCEE
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CO A 1 |
| Chain | Residue |
| A | HIS50 |
| A | HIS122 |
| A | GLU172 |
| A | HOH178 |
| A | HOH179 |
| A | HOH180 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CO B 2 |
| Chain | Residue |
| B | HIS50 |
| B | HIS122 |
| B | GLU172 |
| B | HOH4 |
| B | HOH5 |
| B | HOH6 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CO C 3 |
| Chain | Residue |
| C | HOH7 |
| C | HOH8 |
| C | HOH9 |
| C | HIS50 |
| C | HIS122 |
| C | GLU172 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CO D 4 |
| Chain | Residue |
| D | HOH10 |
| D | HOH11 |
| D | HOH12 |
| D | HIS50 |
| D | HIS122 |
| D | GLU172 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 177 |
| Chain | Residue |
| A | SER-1 |
| A | EDO2 |
| A | ASP136 |
| B | ILE68 |
| B | LEU69 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 2 |
| Chain | Residue |
| A | SER-1 |
| A | ASP136 |
| A | EDO177 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 3 |
| Chain | Residue |
| A | EDO9 |
| A | ALA62 |
| A | LYS66 |
| A | SER74 |
| A | VAL87 |
| A | HOH235 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO D 177 |
| Chain | Residue |
| D | ILE108 |
| D | HIS122 |
| D | PHE160 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D 5 |
| Chain | Residue |
| C | ASN131 |
| C | MET135 |
| C | HOH298 |
| D | ASN131 |
| D | VAL149 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO C 6 |
| Chain | Residue |
| C | HIS121 |
| C | PHE160 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 7 |
| Chain | Residue |
| A | LEU69 |
| B | MET0 |
| B | LEU45 |
| B | ASP136 |
| B | HOH244 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 8 |
| Chain | Residue |
| A | PRO107 |
| A | HIS121 |
| A | HIS122 |
| A | HOH180 |
| A | HOH259 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 9 |
| Chain | Residue |
| A | EDO3 |
| A | LYS66 |
| A | ASN67 |
| site_id | BC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO B 10 |
| Chain | Residue |
| A | PHE64 |
| B | HIS162 |
| B | LYS164 |
| B | ASP165 |
| B | CYS166 |
| B | GLY167 |
| B | GLY168 |
| B | VAL169 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 11 |
| Chain | Residue |
| A | ASN90 |
| A | HOH255 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 12 |
| Chain | Residue |
| A | ASN131 |
| A | VAL149 |
| A | HOH340 |
| B | ASN131 |
| B | MET135 |
| B | HOH203 |
| site_id | BC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 13 |
| Chain | Residue |
| B | GLY46 |
| B | ARG47 |
| B | HOH254 |
| B | HOH320 |
| D | GLN72 |
| D | ASN90 |
| D | GLY92 |
| site_id | BC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO B 14 |
| Chain | Residue |
| B | LYS66 |
| B | ASN67 |
| site_id | CC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO B 15 |
| Chain | Residue |
| B | GLU81 |
| site_id | CC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO B 16 |
| Chain | Residue |
| A | ASN131 |
| B | ASN131 |
| site_id | CC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO C 17 |
| Chain | Residue |
| C | MET0 |
| C | HOH15 |
| C | LEU45 |
| C | ASP136 |
| D | LEU69 |
| site_id | CC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO D 18 |
| Chain | Residue |
| C | LEU69 |
| D | MET0 |
| D | ASP136 |
| D | HOH301 |
| site_id | CC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO C 19 |
| Chain | Residue |
| C | LEU91 |
| C | GLY92 |
| C | HOH180 |
| D | HOH285 |
| C | ASN90 |
| site_id | CC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO C 20 |
| Chain | Residue |
| C | ASN90 |
| C | LYS95 |
| C | HOH187 |
| site_id | CC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO C 21 |
| Chain | Residue |
| B | ARG47 |
| C | LEU45 |
| C | GLY46 |
| D | ALA71 |
| D | GLN72 |
| D | ASN90 |
| D | LEU91 |
| site_id | CC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO C 22 |
| Chain | Residue |
| C | ASP128 |
| C | HOH198 |
| site_id | CC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO C 23 |
| Chain | Residue |
| C | ALA62 |
| C | LYS66 |
| C | SER74 |
| site_id | DC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PG4 D 1 |
| Chain | Residue |
| D | LYS66 |
| D | ASN67 |
| D | VAL73 |
| D | SER74 |
| D | HOH194 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 516 |
| Details | Domain: {"description":"VOC","evidences":[{"source":"PROSITE-ProRule","id":"PRU01163","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"APR-2011","submissionDatabase":"PDB data bank","title":"Crystal structure of human methylmalonyl-CoA epimerase, MCEE.","authoringGroup":["Structural genomics consortium (SGC)"]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9D1I5","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9D1I5","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
