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 |