4PCU
Crystal structure of delta516-525 E201S human cystathionine beta-synthase with AdoMet
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004122 | molecular_function | cystathionine beta-synthase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006534 | biological_process | cysteine metabolic process |
| A | 0006535 | biological_process | cysteine biosynthetic process from serine |
| A | 0006563 | biological_process | L-serine metabolic process |
| A | 0006565 | biological_process | L-serine catabolic process |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0019343 | biological_process | cysteine biosynthetic process via cystathionine |
| A | 0019344 | biological_process | cysteine biosynthetic process |
| A | 0019346 | biological_process | transsulfuration |
| A | 0019448 | biological_process | L-cysteine catabolic process |
| A | 0019825 | molecular_function | oxygen binding |
| A | 0019899 | molecular_function | enzyme binding |
| A | 0020037 | molecular_function | heme binding |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0031625 | molecular_function | ubiquitin protein ligase binding |
| A | 0031667 | biological_process | response to nutrient levels |
| A | 0042262 | biological_process | DNA protection |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0043066 | biological_process | negative regulation of apoptotic process |
| A | 0043418 | biological_process | homocysteine catabolic process |
| A | 0044272 | biological_process | sulfur compound biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050421 | molecular_function | nitrite reductase (NO-forming) activity |
| A | 0050667 | biological_process | homocysteine metabolic process |
| A | 0070025 | molecular_function | carbon monoxide binding |
| A | 0070026 | molecular_function | nitric oxide binding |
| A | 0070814 | biological_process | hydrogen sulfide biosynthetic process |
| A | 0071456 | biological_process | cellular response to hypoxia |
| A | 0072341 | molecular_function | modified amino acid binding |
| A | 1904047 | molecular_function | S-adenosyl-L-methionine binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004122 | molecular_function | cystathionine beta-synthase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006534 | biological_process | cysteine metabolic process |
| B | 0006535 | biological_process | cysteine biosynthetic process from serine |
| B | 0006563 | biological_process | L-serine metabolic process |
| B | 0006565 | biological_process | L-serine catabolic process |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0019343 | biological_process | cysteine biosynthetic process via cystathionine |
| B | 0019344 | biological_process | cysteine biosynthetic process |
| B | 0019346 | biological_process | transsulfuration |
| B | 0019448 | biological_process | L-cysteine catabolic process |
| B | 0019825 | molecular_function | oxygen binding |
| B | 0019899 | molecular_function | enzyme binding |
| B | 0020037 | molecular_function | heme binding |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0031625 | molecular_function | ubiquitin protein ligase binding |
| B | 0031667 | biological_process | response to nutrient levels |
| B | 0042262 | biological_process | DNA protection |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0043066 | biological_process | negative regulation of apoptotic process |
| B | 0043418 | biological_process | homocysteine catabolic process |
| B | 0044272 | biological_process | sulfur compound biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050421 | molecular_function | nitrite reductase (NO-forming) activity |
| B | 0050667 | biological_process | homocysteine metabolic process |
| B | 0070025 | molecular_function | carbon monoxide binding |
| B | 0070026 | molecular_function | nitric oxide binding |
| B | 0070814 | biological_process | hydrogen sulfide biosynthetic process |
| B | 0071456 | biological_process | cellular response to hypoxia |
| B | 0072341 | molecular_function | modified amino acid binding |
| B | 1904047 | molecular_function | S-adenosyl-L-methionine binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | binding site for residue HEM A 601 |
| Chain | Residue |
| A | PRO49 |
| A | PRO64 |
| A | HIS65 |
| A | ALA226 |
| A | PRO229 |
| A | TYR233 |
| A | GLY263 |
| A | ARG266 |
| A | THR313 |
| B | ARG58 |
| B | HEM601 |
| A | SER50 |
| A | ARG51 |
| A | CYS52 |
| A | THR53 |
| A | TRP54 |
| A | PRO59 |
| A | GLU62 |
| A | SER63 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue PLP A 602 |
| Chain | Residue |
| A | LYS119 |
| A | ASN149 |
| A | SER254 |
| A | GLY256 |
| A | THR257 |
| A | GLY258 |
| A | THR260 |
| A | GLU304 |
| A | GLY305 |
| A | ILE306 |
| A | SER349 |
| A | PRO375 |
| A | ASP376 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | binding site for residue SAM A 603 |
| Chain | Residue |
| A | ALA421 |
| A | PRO422 |
| A | LEU423 |
| A | GLY442 |
| A | PHE443 |
| A | ASP444 |
| A | GLN445 |
| A | VAL533 |
| A | THR535 |
| A | ILE537 |
| A | ASP538 |
| B | SAM603 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | binding site for residue HEM B 601 |
| Chain | Residue |
| A | ARG58 |
| A | HEM601 |
| B | PRO49 |
| B | SER50 |
| B | ARG51 |
| B | CYS52 |
| B | THR53 |
| B | TRP54 |
| B | PRO59 |
| B | GLU62 |
| B | SER63 |
| B | PRO64 |
| B | HIS65 |
| B | ARG224 |
| B | ALA226 |
| B | PRO229 |
| B | TYR233 |
| B | GLY263 |
| B | ARG266 |
| B | THR313 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | binding site for residue PLP B 602 |
| Chain | Residue |
| B | LYS119 |
| B | ASN149 |
| B | SER254 |
| B | GLY256 |
| B | THR257 |
| B | GLY258 |
| B | THR260 |
| B | GLU304 |
| B | GLY305 |
| B | ILE306 |
| B | SER349 |
| B | PRO375 |
| B | ASP376 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | binding site for residue SAM B 603 |
| Chain | Residue |
| A | GLY442 |
| A | ASP444 |
| A | SAM603 |
| B | LEU423 |
| B | GLY442 |
| B | PHE443 |
| B | ASP444 |
| B | GLN445 |
| B | VAL533 |
| B | THR535 |
| B | ILE537 |
| B | ASP538 |
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 | 116 |
| Details | Domain: {"description":"CBS","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| 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_FI3 |
| Number of Residues | 12 |
| 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_FI4 |
| Number of Residues | 2 |
| 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_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| 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 | 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 |
