6GPJ
Crystal structure of human GDP-D-mannose 4,6-dehydratase in complex with GDP-4F-Man
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0007219 | biological_process | Notch signaling pathway |
A | 0008446 | molecular_function | GDP-mannose 4,6-dehydratase activity |
A | 0016829 | molecular_function | lyase activity |
A | 0019673 | biological_process | GDP-mannose metabolic process |
A | 0042350 | biological_process | GDP-L-fucose biosynthetic process |
A | 0042351 | biological_process | 'de novo' GDP-L-fucose biosynthetic process |
A | 0042802 | molecular_function | identical protein binding |
A | 0070062 | cellular_component | extracellular exosome |
A | 0070401 | molecular_function | NADP+ binding |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0007219 | biological_process | Notch signaling pathway |
B | 0008446 | molecular_function | GDP-mannose 4,6-dehydratase activity |
B | 0016829 | molecular_function | lyase activity |
B | 0019673 | biological_process | GDP-mannose metabolic process |
B | 0042350 | biological_process | GDP-L-fucose biosynthetic process |
B | 0042351 | biological_process | 'de novo' GDP-L-fucose biosynthetic process |
B | 0042802 | molecular_function | identical protein binding |
B | 0070062 | cellular_component | extracellular exosome |
B | 0070401 | molecular_function | NADP+ binding |
C | 0005515 | molecular_function | protein binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0007219 | biological_process | Notch signaling pathway |
C | 0008446 | molecular_function | GDP-mannose 4,6-dehydratase activity |
C | 0016829 | molecular_function | lyase activity |
C | 0019673 | biological_process | GDP-mannose metabolic process |
C | 0042350 | biological_process | GDP-L-fucose biosynthetic process |
C | 0042351 | biological_process | 'de novo' GDP-L-fucose biosynthetic process |
C | 0042802 | molecular_function | identical protein binding |
C | 0070062 | cellular_component | extracellular exosome |
C | 0070401 | molecular_function | NADP+ binding |
D | 0005515 | molecular_function | protein binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0007219 | biological_process | Notch signaling pathway |
D | 0008446 | molecular_function | GDP-mannose 4,6-dehydratase activity |
D | 0016829 | molecular_function | lyase activity |
D | 0019673 | biological_process | GDP-mannose metabolic process |
D | 0042350 | biological_process | GDP-L-fucose biosynthetic process |
D | 0042351 | biological_process | 'de novo' GDP-L-fucose biosynthetic process |
D | 0042802 | molecular_function | identical protein binding |
D | 0070062 | cellular_component | extracellular exosome |
D | 0070401 | molecular_function | NADP+ binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | binding site for residue CIT A 401 |
Chain | Residue |
A | ASN217 |
A | LYS222 |
A | TYR323 |
A | HOH538 |
A | HOH549 |
A | HOH574 |
B | TYR84 |
site_id | AC2 |
Number of Residues | 29 |
Details | binding site for residue G4F A 402 |
Chain | Residue |
A | THR155 |
A | SER156 |
A | GLU157 |
A | TYR179 |
A | ASN208 |
A | ARG214 |
A | ASN217 |
A | PHE218 |
A | VAL219 |
A | LYS222 |
A | LEU240 |
A | GLY241 |
A | ASN242 |
A | ALA245 |
A | ARG247 |
A | VAL281 |
A | TYR323 |
A | ARG325 |
A | GLU328 |
A | LEU332 |
A | NAP403 |
A | HOH549 |
A | HOH558 |
A | HOH577 |
A | HOH590 |
A | HOH597 |
A | HOH638 |
A | SER112 |
A | VAL114 |
site_id | AC3 |
Number of Residues | 39 |
Details | binding site for residue NAP A 403 |
Chain | Residue |
A | GLY30 |
A | THR32 |
A | GLY33 |
A | GLN34 |
A | ASP35 |
A | ARG55 |
A | ASP86 |
A | LEU87 |
A | LEU108 |
A | GLY109 |
A | ALA110 |
A | SER112 |
A | TYR123 |
A | VAL127 |
A | ALA153 |
A | SER154 |
A | THR155 |
A | TYR179 |
A | LYS183 |
A | LEU206 |
A | ASN208 |
A | HIS209 |
A | ARG214 |
A | G4F402 |
A | HOH540 |
A | HOH552 |
A | HOH577 |
A | HOH584 |
A | HOH585 |
A | HOH596 |
A | HOH598 |
A | HOH601 |
A | HOH605 |
A | HOH624 |
A | HOH631 |
B | ARG56 |
B | SER57 |
B | SER58 |
B | HOH503 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue EDO D 401 |
Chain | Residue |
D | TYR187 |
D | ASP270 |
D | HOH541 |
site_id | AC5 |
Number of Residues | 27 |
Details | binding site for residue G4F D 402 |
Chain | Residue |
D | HOH543 |
D | HOH567 |
D | HOH573 |
D | HOH584 |
D | HOH586 |
D | HOH631 |
D | SER112 |
D | VAL114 |
D | THR155 |
D | SER156 |
D | GLU157 |
D | TYR179 |
D | ASN208 |
D | ARG214 |
D | ASN217 |
D | VAL219 |
D | LYS222 |
D | LEU240 |
D | GLY241 |
D | ASN242 |
D | ALA245 |
D | ARG247 |
D | VAL281 |
D | ARG325 |
D | GLU328 |
D | LEU332 |
D | NAP403 |
site_id | AC6 |
Number of Residues | 39 |
Details | binding site for residue NAP D 403 |
Chain | Residue |
C | ARG56 |
C | SER57 |
C | SER58 |
C | HOH506 |
C | HOH569 |
D | GLY30 |
D | THR32 |
D | GLY33 |
D | GLN34 |
D | ASP35 |
D | ARG55 |
D | ASP86 |
D | LEU87 |
D | LEU108 |
D | GLY109 |
D | ALA110 |
D | SER112 |
D | TYR123 |
D | VAL127 |
D | ALA153 |
D | SER154 |
D | THR155 |
D | TYR179 |
D | LYS183 |
D | LEU206 |
D | ASN208 |
D | HIS209 |
D | ARG214 |
D | G4F402 |
D | HOH519 |
D | HOH528 |
D | HOH542 |
D | HOH543 |
D | HOH565 |
D | HOH572 |
D | HOH594 |
D | HOH596 |
D | HOH604 |
D | HOH607 |
site_id | AC7 |
Number of Residues | 28 |
Details | binding site for residue G4F C 401 |
Chain | Residue |
C | SER112 |
C | VAL114 |
C | THR155 |
C | SER156 |
C | GLU157 |
C | TYR179 |
C | ASN208 |
C | ARG214 |
C | ASN217 |
C | PHE218 |
C | VAL219 |
C | LYS222 |
C | LEU240 |
C | GLY241 |
C | ASN242 |
C | ALA245 |
C | ARG247 |
C | VAL281 |
C | ARG325 |
C | GLU328 |
C | LEU332 |
C | NAP402 |
C | HOH534 |
C | HOH560 |
C | HOH601 |
C | HOH605 |
C | HOH610 |
C | HOH614 |
site_id | AC8 |
Number of Residues | 39 |
Details | binding site for residue NAP C 402 |
Chain | Residue |
C | GLY30 |
C | THR32 |
C | GLY33 |
C | GLN34 |
C | ASP35 |
C | ARG55 |
C | ASP86 |
C | LEU87 |
C | LEU108 |
C | GLY109 |
C | ALA110 |
C | SER112 |
C | TYR123 |
C | VAL127 |
C | ALA153 |
C | SER154 |
C | THR155 |
C | TYR179 |
C | LYS183 |
C | LEU206 |
C | ASN208 |
C | HIS209 |
C | ARG214 |
C | G4F401 |
C | HOH509 |
C | HOH522 |
C | HOH559 |
C | HOH560 |
C | HOH575 |
C | HOH586 |
C | HOH590 |
C | HOH592 |
C | HOH596 |
C | HOH597 |
C | HOH599 |
D | ARG56 |
D | SER57 |
D | SER58 |
D | HOH559 |
site_id | AC9 |
Number of Residues | 8 |
Details | binding site for residue EDO B 401 |
Chain | Residue |
A | HOH520 |
B | SER57 |
B | SER58 |
B | SER59 |
B | ASN61 |
B | HOH595 |
B | HOH638 |
B | HOH665 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue CIT B 402 |
Chain | Residue |
A | TYR84 |
B | ASN217 |
B | LYS222 |
B | TYR323 |
B | HOH576 |
site_id | AD2 |
Number of Residues | 28 |
Details | binding site for residue G4F B 403 |
Chain | Residue |
B | SER112 |
B | VAL114 |
B | THR155 |
B | SER156 |
B | GLU157 |
B | TYR179 |
B | ASN208 |
B | ARG214 |
B | ASN217 |
B | PHE218 |
B | VAL219 |
B | LYS222 |
B | LEU240 |
B | GLY241 |
B | ASN242 |
B | ALA245 |
B | ARG247 |
B | VAL281 |
B | ARG325 |
B | GLU328 |
B | LEU332 |
B | NAP404 |
B | HOH530 |
B | HOH561 |
B | HOH564 |
B | HOH576 |
B | HOH581 |
B | HOH629 |
site_id | AD3 |
Number of Residues | 39 |
Details | binding site for residue NAP B 404 |
Chain | Residue |
A | ARG56 |
A | SER57 |
A | SER58 |
A | HOH509 |
B | GLY30 |
B | THR32 |
B | GLY33 |
B | GLN34 |
B | ASP35 |
B | ARG55 |
B | ASP86 |
B | LEU87 |
B | LEU108 |
B | GLY109 |
B | ALA110 |
B | SER112 |
B | TYR123 |
B | VAL127 |
B | ALA153 |
B | SER154 |
B | THR155 |
B | TYR179 |
B | LYS183 |
B | LEU206 |
B | ASN208 |
B | HIS209 |
B | ARG214 |
B | G4F403 |
B | HOH530 |
B | HOH534 |
B | HOH538 |
B | HOH558 |
B | HOH560 |
B | HOH580 |
B | HOH597 |
B | HOH601 |
B | HOH631 |
B | HOH634 |
B | HOH656 |
Functional Information from PROSITE/UniProt
site_id | PS00061 |
Number of Residues | 29 |
Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. PqkettpfypRspYGAAKLYAyWIVvNFR |
Chain | Residue | Details |
A | PRO166-ARG194 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: ACT_SITE => ECO:0000250 |
Chain | Residue | Details |
A | THR155 | |
D | THR155 | |
C | THR155 | |
B | THR155 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | ACT_SITE: Nucleophile => ECO:0000250 |
Chain | Residue | Details |
A | GLU157 | |
A | TYR179 | |
D | GLU157 | |
D | TYR179 | |
C | GLU157 | |
C | TYR179 | |
B | GLU157 | |
B | TYR179 |
site_id | SWS_FT_FI3 |
Number of Residues | 32 |
Details | BINDING: BINDING => ECO:0000269|Ref.9 |
Chain | Residue | Details |
A | GLY30 | |
D | ARG55 | |
D | ASP86 | |
D | LEU108 | |
D | TYR123 | |
D | LYS183 | |
D | HIS209 | |
D | ARG214 | |
C | GLY30 | |
C | ARG55 | |
C | ASP86 | |
A | ARG55 | |
C | LEU108 | |
C | TYR123 | |
C | LYS183 | |
C | HIS209 | |
C | ARG214 | |
B | GLY30 | |
B | ARG55 | |
B | ASP86 | |
B | LEU108 | |
B | TYR123 | |
A | ASP86 | |
B | LYS183 | |
B | HIS209 | |
B | ARG214 | |
A | LEU108 | |
A | TYR123 | |
A | LYS183 | |
A | HIS209 | |
A | ARG214 | |
D | GLY30 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | TYR323 | |
D | TYR323 | |
C | TYR323 | |
B | TYR323 |