5M67
Crystal structure of S-adenosyl-L-homocysteine hydrolase from Bradyrhizobium elkanii in complex with adenine and 2'-deoxyadenosine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004013 | molecular_function | adenosylhomocysteinase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006730 | biological_process | one-carbon metabolic process |
A | 0016787 | molecular_function | hydrolase activity |
A | 0071269 | biological_process | L-homocysteine biosynthetic process |
B | 0004013 | molecular_function | adenosylhomocysteinase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0006730 | biological_process | one-carbon metabolic process |
B | 0016787 | molecular_function | hydrolase activity |
B | 0071269 | biological_process | L-homocysteine biosynthetic process |
C | 0004013 | molecular_function | adenosylhomocysteinase activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0006730 | biological_process | one-carbon metabolic process |
C | 0016787 | molecular_function | hydrolase activity |
C | 0071269 | biological_process | L-homocysteine biosynthetic process |
D | 0004013 | molecular_function | adenosylhomocysteinase activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0006730 | biological_process | one-carbon metabolic process |
D | 0016787 | molecular_function | hydrolase activity |
D | 0071269 | biological_process | L-homocysteine biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue NA A 501 |
Chain | Residue |
A | GLN62 |
A | MET390 |
A | HIS392 |
A | HOH878 |
A | HOH922 |
C | HOH814 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue NA A 502 |
Chain | Residue |
C | HOH807 |
D | HOH791 |
D | HOH994 |
A | HOH846 |
A | HOH1038 |
B | HOH783 |
site_id | AC3 |
Number of Residues | 33 |
Details | binding site for residue NAD A 503 |
Chain | Residue |
A | THR198 |
A | THR199 |
A | THR200 |
A | ASN232 |
A | GLY263 |
A | ASP264 |
A | VAL265 |
A | SER283 |
A | GLU284 |
A | VAL285 |
A | ASP286 |
A | CYS289 |
A | THR317 |
A | GLY318 |
A | ASN319 |
A | ILE322 |
A | ILE340 |
A | GLY341 |
A | HIS342 |
A | LEU383 |
A | ASN385 |
A | HIS392 |
A | ADE504 |
A | HOH696 |
A | HOH747 |
A | HOH749 |
A | HOH766 |
A | HOH782 |
A | HOH829 |
A | HOH862 |
B | GLN454 |
B | LYS467 |
B | TYR471 |
site_id | AC4 |
Number of Residues | 13 |
Details | binding site for residue ADE A 504 |
Chain | Residue |
A | HIS58 |
A | THR60 |
A | GLN62 |
A | THR63 |
A | LEU386 |
A | MET390 |
A | HIS392 |
A | MET397 |
A | PHE401 |
A | NAD503 |
A | HOH604 |
A | HOH729 |
A | HOH835 |
site_id | AC5 |
Number of Residues | 10 |
Details | binding site for residue PEG A 505 |
Chain | Residue |
A | ARG237 |
A | GLN275 |
A | HOH603 |
A | HOH620 |
A | HOH812 |
A | HOH970 |
C | ARG245 |
C | GLN275 |
C | ALA276 |
C | GLY277 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue NA B 501 |
Chain | Residue |
B | GLN62 |
B | MET390 |
B | HIS392 |
B | HOH847 |
B | HOH899 |
D | HOH842 |
site_id | AC7 |
Number of Residues | 34 |
Details | binding site for residue NAD B 502 |
Chain | Residue |
B | HIS392 |
B | ADE503 |
B | HOH662 |
B | HOH671 |
B | HOH677 |
B | HOH778 |
B | HOH801 |
B | HOH811 |
B | HOH957 |
A | LYS467 |
A | TYR471 |
B | THR198 |
B | THR199 |
B | THR200 |
B | ASN232 |
B | GLY261 |
B | GLY263 |
B | ASP264 |
B | VAL265 |
B | SER283 |
B | GLU284 |
B | VAL285 |
B | ASP286 |
B | CYS289 |
B | ALA316 |
B | THR317 |
B | GLY318 |
B | ASN319 |
B | ILE322 |
B | ILE340 |
B | GLY341 |
B | HIS342 |
B | LEU383 |
B | ASN385 |
site_id | AC8 |
Number of Residues | 12 |
Details | binding site for residue ADE B 503 |
Chain | Residue |
B | HIS58 |
B | THR60 |
B | GLN62 |
B | THR63 |
B | MET390 |
B | HIS392 |
B | MET397 |
B | PHE401 |
B | NAD502 |
B | HOH614 |
B | HOH641 |
B | HOH709 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue PEG B 504 |
Chain | Residue |
B | PHE20 |
B | LYS23 |
B | HOH685 |
B | HOH766 |
D | ILE360 |
D | LYS361 |
D | HOH816 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue ACT B 505 |
Chain | Residue |
B | ASP344 |
B | ILE349 |
B | ARG353 |
B | ARG382 |
B | HOH687 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue NA C 501 |
Chain | Residue |
A | HOH828 |
C | GLN62 |
C | MET390 |
C | HIS392 |
C | HOH791 |
C | HOH878 |
site_id | AD3 |
Number of Residues | 33 |
Details | binding site for residue NAD C 502 |
Chain | Residue |
C | THR198 |
C | THR199 |
C | THR200 |
C | ASN232 |
C | GLY263 |
C | ASP264 |
C | VAL265 |
C | SER283 |
C | GLU284 |
C | VAL285 |
C | ASP286 |
C | CYS289 |
C | THR317 |
C | GLY318 |
C | ASN319 |
C | ILE322 |
C | ILE340 |
C | GLY341 |
C | HIS342 |
C | LEU383 |
C | ASN385 |
C | HIS392 |
C | 3D1503 |
C | HOH696 |
C | HOH717 |
C | HOH722 |
C | HOH726 |
C | HOH733 |
C | HOH759 |
C | HOH800 |
D | GLN454 |
D | LYS467 |
D | TYR471 |
site_id | AD4 |
Number of Residues | 18 |
Details | binding site for residue 3D1 C 503 |
Chain | Residue |
C | LEU57 |
C | HIS58 |
C | THR60 |
C | GLN62 |
C | THR63 |
C | ASP135 |
C | GLU197 |
C | THR198 |
C | LYS227 |
C | ASP231 |
C | HIS342 |
C | LEU383 |
C | MET390 |
C | HIS392 |
C | MET397 |
C | PHE401 |
C | NAD502 |
C | HOH609 |
site_id | AD5 |
Number of Residues | 6 |
Details | binding site for residue ACT C 504 |
Chain | Residue |
C | ASP344 |
C | ILE349 |
C | ARG353 |
C | ARG382 |
C | HOH601 |
C | HOH645 |
site_id | AD6 |
Number of Residues | 6 |
Details | binding site for residue NA D 501 |
Chain | Residue |
B | HOH815 |
D | GLN62 |
D | MET390 |
D | HIS392 |
D | HOH766 |
D | HOH898 |
site_id | AD7 |
Number of Residues | 34 |
Details | binding site for residue NAD D 502 |
Chain | Residue |
C | LEU450 |
C | GLN454 |
C | LYS467 |
C | TYR471 |
D | THR198 |
D | THR199 |
D | THR200 |
D | ASN232 |
D | GLY263 |
D | ASP264 |
D | VAL265 |
D | SER283 |
D | GLU284 |
D | VAL285 |
D | ASP286 |
D | CYS289 |
D | THR317 |
D | GLY318 |
D | ASN319 |
D | ILE322 |
D | ILE340 |
D | GLY341 |
D | HIS342 |
D | LEU383 |
D | ASN385 |
D | HIS392 |
D | 3D1503 |
D | HOH715 |
D | HOH724 |
D | HOH753 |
D | HOH782 |
D | HOH783 |
D | HOH803 |
D | HOH949 |
site_id | AD8 |
Number of Residues | 17 |
Details | binding site for residue 3D1 D 503 |
Chain | Residue |
D | HIS58 |
D | THR60 |
D | GLN62 |
D | THR63 |
D | ASP135 |
D | GLU197 |
D | THR198 |
D | LYS227 |
D | ASP231 |
D | HIS342 |
D | MET390 |
D | HIS392 |
D | MET397 |
D | PHE401 |
D | NAD502 |
D | HOH609 |
D | HOH621 |
site_id | AD9 |
Number of Residues | 10 |
Details | binding site for residue PEG D 504 |
Chain | Residue |
B | ARG245 |
B | GLN275 |
B | ALA276 |
B | GLY277 |
D | ARG237 |
D | GLN275 |
D | HOH605 |
D | HOH615 |
D | HOH674 |
D | HOH990 |
Functional Information from PROSITE/UniProt
site_id | PS00738 |
Number of Residues | 15 |
Details | ADOHCYASE_1 S-adenosyl-L-homocysteine hydrolase signature 1. SCNiYSTQDhAAAAI |
Chain | Residue | Details |
A | SER81-ILE95 |
site_id | PS00739 |
Number of Residues | 18 |
Details | ADOHCYASE_2 S-adenosyl-L-homocysteine hydrolase signature 2. GKvamVaGFGdVGKGsaA |
Chain | Residue | Details |
A | GLY254-ALA271 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000305|PubMed:26627650 |
Chain | Residue | Details |
A | HIS58 | |
D | HIS58 | |
D | HIS342 | |
D | HIS392 | |
A | HIS342 | |
A | HIS392 | |
B | HIS58 | |
B | HIS342 | |
B | HIS392 | |
C | HIS58 | |
C | HIS342 | |
C | HIS392 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00563, ECO:0000305|PubMed:26627650 |
Chain | Residue | Details |
A | ASP135 | |
C | GLU197 | |
C | LYS227 | |
C | ASP231 | |
D | ASP135 | |
D | GLU197 | |
D | LYS227 | |
D | ASP231 | |
A | GLU197 | |
A | LYS227 | |
A | ASP231 | |
B | ASP135 | |
B | GLU197 | |
B | LYS227 | |
B | ASP231 | |
C | ASP135 |
site_id | SWS_FT_FI3 |
Number of Residues | 20 |
Details | BINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_00563, ECO:0000269|PubMed:26627650 |
Chain | Residue | Details |
A | THR198 | |
B | ASN385 | |
C | THR198 | |
C | ASN232 | |
C | GLU284 | |
C | ILE340 | |
C | ASN385 | |
D | THR198 | |
D | ASN232 | |
D | GLU284 | |
D | ILE340 | |
A | ASN232 | |
D | ASN385 | |
A | GLU284 | |
A | ILE340 | |
A | ASN385 | |
B | THR198 | |
B | ASN232 | |
B | GLU284 | |
B | ILE340 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: in other chain => ECO:0000269|PubMed:26627650 |
Chain | Residue | Details |
A | VAL265 | |
B | VAL265 | |
C | VAL265 | |
D | VAL265 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_00563 |
Chain | Residue | Details |
A | ASN319 | |
B | ASN319 | |
C | ASN319 | |
D | ASN319 |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:26627650 |
Chain | Residue | Details |
A | LYS467 | |
A | TYR471 | |
B | LYS467 | |
B | TYR471 | |
C | LYS467 | |
C | TYR471 | |
D | LYS467 | |
D | TYR471 |