1JBQ
STRUCTURE OF HUMAN CYSTATHIONINE BETA-SYNTHASE: A UNIQUE PYRIDOXAL 5'-PHOSPHATE DEPENDENT HEMEPROTEIN
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 | L-cysteine biosynthetic process from L-serine |
| A | 0019343 | biological_process | L-cysteine biosynthetic process via L-cystathionine |
| B | 0004122 | molecular_function | cystathionine beta-synthase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006535 | biological_process | L-cysteine biosynthetic process from L-serine |
| B | 0019343 | biological_process | L-cysteine biosynthetic process via L-cystathionine |
| C | 0004122 | molecular_function | cystathionine beta-synthase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006535 | biological_process | L-cysteine biosynthetic process from L-serine |
| C | 0019343 | biological_process | L-cysteine biosynthetic process via L-cystathionine |
| D | 0004122 | molecular_function | cystathionine beta-synthase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006535 | biological_process | L-cysteine biosynthetic process from L-serine |
| D | 0019343 | biological_process | L-cysteine biosynthetic process via L-cystathionine |
| E | 0004122 | molecular_function | cystathionine beta-synthase activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0006535 | biological_process | L-cysteine biosynthetic process from L-serine |
| E | 0019343 | biological_process | L-cysteine biosynthetic process via L-cystathionine |
| F | 0004122 | molecular_function | cystathionine beta-synthase activity |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0006535 | biological_process | L-cysteine biosynthetic process from L-serine |
| F | 0019343 | biological_process | L-cysteine biosynthetic process via L-cystathionine |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEM A 501 |
| Chain | Residue |
| A | SER50 |
| A | ARG224 |
| A | ALA226 |
| A | PRO229 |
| A | LEU230 |
| A | TYR233 |
| A | ARG266 |
| B | THR53 |
| B | ARG58 |
| B | HEM501 |
| A | ARG51 |
| A | CYS52 |
| A | THR53 |
| A | TRP54 |
| A | GLU62 |
| A | SER63 |
| A | PRO64 |
| A | HIS65 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEM B 501 |
| Chain | Residue |
| A | THR53 |
| A | ARG58 |
| A | HEM501 |
| B | SER50 |
| B | ARG51 |
| B | CYS52 |
| B | THR53 |
| B | TRP54 |
| B | GLU62 |
| B | PRO64 |
| B | HIS65 |
| B | ARG224 |
| B | ALA226 |
| B | PRO229 |
| B | LEU230 |
| B | TYR233 |
| B | ARG266 |
| B | HOH1011 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEM C 501 |
| Chain | Residue |
| C | SER50 |
| C | ARG51 |
| C | CYS52 |
| C | THR53 |
| C | TRP54 |
| 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 | HEM501 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEM D 501 |
| Chain | Residue |
| C | THR53 |
| C | ARG58 |
| C | HEM501 |
| C | HOH1004 |
| D | SER50 |
| D | ARG51 |
| D | CYS52 |
| D | THR53 |
| D | TRP54 |
| D | GLU62 |
| D | PRO64 |
| D | HIS65 |
| D | ARG224 |
| D | ALA226 |
| D | PRO229 |
| D | LEU230 |
| D | TYR233 |
| D | ARG266 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEM E 501 |
| Chain | Residue |
| E | ARG51 |
| E | CYS52 |
| E | THR53 |
| E | TRP54 |
| E | GLU62 |
| E | SER63 |
| E | PRO64 |
| E | HIS65 |
| E | ARG224 |
| E | ALA226 |
| E | PRO229 |
| E | LEU230 |
| E | TYR233 |
| E | ARG266 |
| F | THR53 |
| F | ARG58 |
| F | HEM501 |
| site_id | AC6 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEM F 501 |
| Chain | Residue |
| F | PRO64 |
| F | HIS65 |
| F | ARG224 |
| F | ALA226 |
| F | PRO229 |
| F | LEU230 |
| F | TYR233 |
| F | ARG266 |
| E | THR53 |
| E | ARG58 |
| E | HEM501 |
| F | SER50 |
| F | ARG51 |
| F | CYS52 |
| F | THR53 |
| F | TRP54 |
| F | GLU62 |
| F | SER63 |
| site_id | AC7 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PLP A 1001 |
| Chain | Residue |
| A | LYS119 |
| A | ASN149 |
| A | SER254 |
| A | VAL255 |
| A | GLY256 |
| A | THR257 |
| A | GLY258 |
| A | GLY259 |
| A | THR260 |
| A | GLY305 |
| A | ILE306 |
| A | SER349 |
| A | PRO375 |
| A | ASP376 |
| A | TYR381 |
| A | HOH1020 |
| A | HOH1021 |
| site_id | AC8 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP B 1001 |
| Chain | Residue |
| B | LYS119 |
| B | ASN149 |
| B | SER254 |
| B | VAL255 |
| B | GLY256 |
| B | THR257 |
| B | GLY258 |
| B | GLY259 |
| B | THR260 |
| B | GLY305 |
| B | ILE306 |
| B | SER349 |
| B | PRO375 |
| B | ASP376 |
| B | TYR381 |
| B | HOH1029 |
| site_id | AC9 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE PLP C 1001 |
| Chain | Residue |
| C | LYS119 |
| C | ASN149 |
| C | SER254 |
| C | VAL255 |
| C | GLY256 |
| C | THR257 |
| C | GLY258 |
| C | GLY259 |
| C | THR260 |
| C | GLU304 |
| C | GLY305 |
| C | ILE306 |
| C | SER349 |
| C | PRO375 |
| C | ASP376 |
| C | TYR381 |
| C | HOH1006 |
| C | HOH1024 |
| C | HOH1025 |
| site_id | BC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PLP D 1001 |
| Chain | Residue |
| D | LYS119 |
| D | ASN149 |
| 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 | TYR381 |
| D | HOH1023 |
| D | HOH1024 |
| site_id | BC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE PLP E 1001 |
| Chain | Residue |
| E | LYS119 |
| E | ASN149 |
| E | SER254 |
| E | VAL255 |
| E | GLY256 |
| E | THR257 |
| E | GLY258 |
| E | GLY259 |
| E | THR260 |
| E | GLY305 |
| E | SER349 |
| E | PRO375 |
| E | ASP376 |
| E | TYR381 |
| E | HOH1006 |
| E | HOH1028 |
| E | HOH1029 |
| E | HOH1030 |
| site_id | BC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PLP F 1001 |
| Chain | Residue |
| F | LYS119 |
| F | ASN149 |
| F | SER254 |
| F | VAL255 |
| F | GLY256 |
| F | THR257 |
| F | GLY258 |
| F | GLY259 |
| F | THR260 |
| F | GLY305 |
| F | ILE306 |
| F | SER349 |
| F | PRO375 |
| F | ASP376 |
| F | TYR381 |
| F | HOH1020 |
| F | HOH1021 |
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 site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"11483494","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12173932","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11483494","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12173932","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"11483494","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12173932","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)","evidences":[{"source":"PubMed","id":"17087506","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1oas |
| Chain | Residue | Details |
| A | LYS119 | |
| A | SER349 |
| site_id | CSA10 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oas |
| Chain | Residue | Details |
| D | LYS119 |
| site_id | CSA11 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oas |
| Chain | Residue | Details |
| E | LYS119 |
| site_id | CSA12 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oas |
| Chain | Residue | Details |
| F | LYS119 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1oas |
| Chain | Residue | Details |
| B | LYS119 | |
| B | SER349 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1oas |
| Chain | Residue | Details |
| C | LYS119 | |
| C | SER349 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1oas |
| Chain | Residue | Details |
| D | LYS119 | |
| D | SER349 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1oas |
| Chain | Residue | Details |
| E | LYS119 | |
| E | SER349 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1oas |
| Chain | Residue | Details |
| F | LYS119 | |
| F | SER349 |
| site_id | CSA7 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oas |
| Chain | Residue | Details |
| A | LYS119 |
| site_id | CSA8 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oas |
| Chain | Residue | Details |
| B | LYS119 |
| site_id | CSA9 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oas |
| Chain | Residue | Details |
| C | LYS119 |
| 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 |
