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 | 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 | 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: axial binding residue => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932 |
Chain | Residue | Details |
A | THR53 | |
E | HIS66 | |
F | THR53 | |
F | HIS66 | |
A | HIS66 | |
B | THR53 | |
B | HIS66 | |
C | THR53 | |
C | HIS66 | |
D | THR53 | |
D | HIS66 | |
E | THR53 |
site_id | SWS_FT_FI2 |
Number of Residues | 18 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932 |
Chain | Residue | Details |
A | THR150 | |
D | THR150 | |
D | THR257 | |
D | ALA350 | |
E | THR150 | |
E | THR257 | |
E | ALA350 | |
F | THR150 | |
F | THR257 | |
F | ALA350 | |
A | THR257 | |
A | ALA350 | |
B | THR150 | |
B | THR257 | |
B | ALA350 | |
C | THR150 | |
C | THR257 | |
C | ALA350 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692 |
Chain | Residue | Details |
A | LEU28 | |
B | LEU28 | |
C | LEU28 | |
D | LEU28 | |
E | LEU28 | |
F | LEU28 |
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 | ASP120 | |
B | ASP120 | |
C | ASP120 | |
D | ASP120 | |
E | ASP120 | |
F | ASP120 |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | PRO200 | |
B | PRO200 | |
C | PRO200 | |
D | PRO200 | |
E | PRO200 | |
F | PRO200 |
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 | ASN212 | |
F | ASN212 | |
B | ASN212 | |
C | ASN212 | |
D | ASN212 | |
E | ASN212 |
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 | ASP120 | 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 | ASP120 | 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 | ASP120 | 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 | ASP120 | 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 | ASP120 | 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 | ASP120 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |