5MMS
Human cystathionine beta-synthase (CBS) p.P49L delta409-551 variant
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004122 | molecular_function | cystathionine beta-synthase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006535 | biological_process | cysteine biosynthetic process from serine |
| A | 0019343 | biological_process | cysteine biosynthetic process via cystathionine |
| B | 0004122 | molecular_function | cystathionine beta-synthase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006535 | biological_process | cysteine biosynthetic process from serine |
| B | 0019343 | biological_process | cysteine biosynthetic process via cystathionine |
| C | 0004122 | molecular_function | cystathionine beta-synthase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006535 | biological_process | cysteine biosynthetic process from serine |
| C | 0019343 | biological_process | cysteine biosynthetic process via cystathionine |
| D | 0004122 | molecular_function | cystathionine beta-synthase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006535 | biological_process | cysteine biosynthetic process from serine |
| D | 0019343 | biological_process | cysteine biosynthetic process via cystathionine |
| E | 0004122 | molecular_function | cystathionine beta-synthase activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0006535 | biological_process | cysteine biosynthetic process from serine |
| E | 0019343 | biological_process | cysteine biosynthetic process via cystathionine |
| F | 0004122 | molecular_function | cystathionine beta-synthase activity |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0006535 | biological_process | cysteine biosynthetic process from serine |
| F | 0019343 | biological_process | cysteine biosynthetic process via cystathionine |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | binding site for residue HEM A 1001 |
| Chain | Residue |
| A | SER50 |
| A | PRO64 |
| A | HIS65 |
| A | ARG224 |
| A | ALA226 |
| A | PRO229 |
| A | LEU230 |
| A | TYR233 |
| A | ARG266 |
| A | HOH1102 |
| F | THR53 |
| A | ARG51 |
| F | ARG58 |
| A | CYS52 |
| A | THR53 |
| A | TRP54 |
| A | ARG58 |
| A | PRO59 |
| A | GLU62 |
| A | SER63 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue PLP A 1002 |
| Chain | Residue |
| A | LYS119 |
| A | ASN149 |
| A | SER254 |
| A | VAL255 |
| A | GLY256 |
| A | THR257 |
| A | GLY258 |
| A | THR260 |
| A | GLY305 |
| A | ILE306 |
| A | SER349 |
| A | PRO375 |
| A | ASP376 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | binding site for residue HEM B 1001 |
| Chain | Residue |
| B | SER50 |
| B | ARG51 |
| B | CYS52 |
| B | THR53 |
| B | TRP54 |
| B | ARG58 |
| B | PRO59 |
| B | GLU62 |
| B | SER63 |
| B | PRO64 |
| B | HIS65 |
| B | ALA226 |
| B | PRO229 |
| B | LEU230 |
| B | TYR233 |
| B | ARG266 |
| B | HOH1108 |
| B | HOH1114 |
| E | THR53 |
| E | ARG58 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | binding site for residue HEM C 1001 |
| Chain | Residue |
| C | SER50 |
| C | ARG51 |
| C | CYS52 |
| C | THR53 |
| C | TRP54 |
| C | ARG58 |
| C | PRO59 |
| C | GLU62 |
| C | SER63 |
| C | PRO64 |
| C | HIS65 |
| C | ARG224 |
| C | ALA226 |
| C | PRO229 |
| C | LEU230 |
| C | TYR233 |
| C | ARG266 |
| D | THR53 |
| D | ARG58 |
| D | HEM1001 |
| site_id | AC5 |
| Number of Residues | 20 |
| Details | binding site for residue HEM D 1001 |
| Chain | Residue |
| C | THR53 |
| C | ARG58 |
| C | HEM1001 |
| D | SER50 |
| D | ARG51 |
| D | CYS52 |
| D | THR53 |
| D | TRP54 |
| D | ARG58 |
| D | PRO59 |
| D | GLU62 |
| D | SER63 |
| D | PRO64 |
| D | HIS65 |
| D | ARG224 |
| D | ALA226 |
| D | PRO229 |
| D | LEU230 |
| D | TYR233 |
| D | ARG266 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue NA E 501 |
| Chain | Residue |
| D | ASP79 |
| D | ILE80 |
| E | GLU342 |
| site_id | AC7 |
| Number of Residues | 19 |
| Details | binding site for residue HEM E 502 |
| Chain | Residue |
| E | SER50 |
| E | ARG51 |
| E | CYS52 |
| E | THR53 |
| E | ARG58 |
| E | PRO59 |
| E | GLU62 |
| E | SER63 |
| E | PRO64 |
| E | HIS65 |
| E | ALA226 |
| E | PRO229 |
| E | LEU230 |
| E | TYR233 |
| E | ARG266 |
| E | HOH1111 |
| B | THR53 |
| B | ARG58 |
| E | LEU49 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue NA E 504 |
| Chain | Residue |
| E | ILE92 |
| E | GLY96 |
| E | LYS97 |
| E | HOH1101 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue NA F 501 |
| Chain | Residue |
| B | ASP79 |
| B | ILE80 |
| F | GLU342 |
| F | HOH1125 |
| site_id | AD1 |
| Number of Residues | 20 |
| Details | binding site for residue HEM F 502 |
| Chain | Residue |
| A | THR53 |
| A | ARG58 |
| F | SER50 |
| F | ARG51 |
| F | CYS52 |
| F | THR53 |
| F | TRP54 |
| F | ARG58 |
| F | PRO59 |
| F | GLU62 |
| F | SER63 |
| F | PRO64 |
| F | HIS65 |
| F | ARG224 |
| F | ALA226 |
| F | PRO229 |
| F | LEU230 |
| F | TYR233 |
| F | ARG266 |
| F | HOH1123 |
| site_id | AD2 |
| Number of Residues | 22 |
| Details | binding site for Di-peptide PLP B 1002 and LYS B 119 |
| Chain | Residue |
| B | SER117 |
| B | VAL118 |
| B | ASP120 |
| B | ARG121 |
| B | ILE122 |
| B | SER123 |
| B | ASN149 |
| B | THR150 |
| B | SER254 |
| B | VAL255 |
| B | GLY256 |
| B | THR257 |
| B | GLY258 |
| B | THR260 |
| B | GLY305 |
| B | ILE306 |
| B | SER349 |
| B | PRO375 |
| B | ASP376 |
| B | HOH1106 |
| B | HOH1119 |
| B | HOH1127 |
| site_id | AD3 |
| Number of Residues | 21 |
| Details | binding site for Di-peptide PLP C 1002 and LYS C 119 |
| Chain | Residue |
| C | SER117 |
| C | VAL118 |
| C | ASP120 |
| C | ARG121 |
| C | ILE122 |
| C | SER123 |
| C | ASN149 |
| C | THR150 |
| C | VAL255 |
| C | GLY256 |
| C | THR257 |
| C | GLY258 |
| C | THR260 |
| C | GLY305 |
| C | ILE306 |
| C | SER349 |
| C | PRO375 |
| C | ASP376 |
| C | TYR381 |
| C | HOH1101 |
| C | HOH1109 |
| site_id | AD4 |
| Number of Residues | 21 |
| Details | binding site for Di-peptide PLP D 1002 and LYS D 119 |
| Chain | Residue |
| D | SER117 |
| D | VAL118 |
| D | ASP120 |
| D | ARG121 |
| D | ILE122 |
| D | SER123 |
| D | ASN149 |
| D | THR150 |
| D | SER254 |
| D | VAL255 |
| D | GLY256 |
| D | THR257 |
| D | GLY258 |
| D | GLY259 |
| D | THR260 |
| D | GLY305 |
| D | ILE306 |
| D | SER349 |
| D | PRO375 |
| D | ASP376 |
| D | HOH1107 |
| site_id | AD5 |
| Number of Residues | 19 |
| Details | binding site for Di-peptide PLP E 503 and LYS E 119 |
| Chain | Residue |
| E | SER117 |
| E | VAL118 |
| E | ASP120 |
| E | ARG121 |
| E | ILE122 |
| E | SER123 |
| E | ASN149 |
| E | THR150 |
| E | SER254 |
| E | VAL255 |
| E | GLY256 |
| E | THR257 |
| E | GLY258 |
| E | THR260 |
| E | GLY305 |
| E | ILE306 |
| E | SER349 |
| E | PRO375 |
| E | ASP376 |
| site_id | AD6 |
| Number of Residues | 19 |
| Details | binding site for Di-peptide PLP F 503 and LYS F 119 |
| Chain | Residue |
| F | SER117 |
| F | VAL118 |
| F | ASP120 |
| F | ARG121 |
| F | ILE122 |
| F | SER123 |
| F | ASN149 |
| F | THR150 |
| F | SER254 |
| F | VAL255 |
| F | GLY256 |
| F | THR257 |
| F | GLY258 |
| F | THR260 |
| F | GLY305 |
| F | ILE306 |
| F | SER349 |
| F | PRO375 |
| F | ASP376 |
Functional Information from PROSITE/UniProt
| site_id | PS00901 |
| Number of Residues | 19 |
| Details | CYS_SYNTHASE Cysteine synthase/cystathionine beta-synthase P-phosphate attachment site. KcEffn.AGgSVKdRiSlrM |
| Chain | Residue | Details |
| A | LYS108-MET126 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: axial binding residue => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932 |
| Chain | Residue | Details |
| A | CYS52 | |
| E | HIS65 | |
| F | CYS52 | |
| F | HIS65 | |
| A | HIS65 | |
| B | CYS52 | |
| B | HIS65 | |
| C | CYS52 | |
| C | HIS65 | |
| D | CYS52 | |
| D | HIS65 | |
| E | CYS52 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932 |
| Chain | Residue | Details |
| A | ASN149 | |
| D | ASN149 | |
| D | GLY256 | |
| D | SER349 | |
| E | ASN149 | |
| E | GLY256 | |
| E | SER349 | |
| F | ASN149 | |
| F | GLY256 | |
| F | SER349 | |
| A | GLY256 | |
| A | SER349 | |
| B | ASN149 | |
| B | GLY256 | |
| B | SER349 | |
| C | ASN149 | |
| C | GLY256 | |
| C | SER349 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692 |
| Chain | Residue | Details |
| A | SER27 | |
| B | SER27 | |
| C | SER27 | |
| D | SER27 | |
| E | SER27 | |
| F | SER27 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932 |
| Chain | Residue | Details |
| A | LYS119 | |
| B | LYS119 | |
| C | LYS119 | |
| D | LYS119 | |
| E | LYS119 | |
| F | LYS119 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER199 | |
| B | SER199 | |
| C | SER199 | |
| D | SER199 | |
| E | SER199 | |
| F | SER199 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 12 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:17087506 |
| Chain | Residue | Details |
| A | LYS211 | |
| F | LYS211 | |
| B | LYS211 | |
| C | LYS211 | |
| D | LYS211 | |
| E | LYS211 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 1 |
| Details | M-CSA 713 |
| Chain | Residue | Details |
| A | LYS119 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
| site_id | MCSA2 |
| Number of Residues | 1 |
| Details | M-CSA 713 |
| Chain | Residue | Details |
| B | LYS119 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
| site_id | MCSA3 |
| Number of Residues | 1 |
| Details | M-CSA 713 |
| Chain | Residue | Details |
| C | LYS119 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
| site_id | MCSA4 |
| Number of Residues | 1 |
| Details | M-CSA 713 |
| Chain | Residue | Details |
| D | LYS119 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
| site_id | MCSA5 |
| Number of Residues | 1 |
| Details | M-CSA 713 |
| Chain | Residue | Details |
| E | LYS119 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
| site_id | MCSA6 |
| Number of Residues | 1 |
| Details | M-CSA 713 |
| Chain | Residue | Details |
| F | LYS119 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
