3EBL
Crystal Structure of Rice GID1 complexed with GA4
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0009739 | biological_process | response to gibberellin |
A | 0009740 | biological_process | gibberellic acid mediated signaling pathway |
A | 0009939 | biological_process | positive regulation of gibberellic acid mediated signaling pathway |
A | 0010325 | biological_process | raffinose family oligosaccharide biosynthetic process |
A | 0010331 | molecular_function | gibberellin binding |
A | 0016787 | molecular_function | hydrolase activity |
A | 0048444 | biological_process | floral organ morphogenesis |
B | 0005634 | cellular_component | nucleus |
B | 0005737 | cellular_component | cytoplasm |
B | 0009739 | biological_process | response to gibberellin |
B | 0009740 | biological_process | gibberellic acid mediated signaling pathway |
B | 0009939 | biological_process | positive regulation of gibberellic acid mediated signaling pathway |
B | 0010325 | biological_process | raffinose family oligosaccharide biosynthetic process |
B | 0010331 | molecular_function | gibberellin binding |
B | 0016787 | molecular_function | hydrolase activity |
B | 0048444 | biological_process | floral organ morphogenesis |
C | 0005634 | cellular_component | nucleus |
C | 0005737 | cellular_component | cytoplasm |
C | 0009739 | biological_process | response to gibberellin |
C | 0009740 | biological_process | gibberellic acid mediated signaling pathway |
C | 0009939 | biological_process | positive regulation of gibberellic acid mediated signaling pathway |
C | 0010325 | biological_process | raffinose family oligosaccharide biosynthetic process |
C | 0010331 | molecular_function | gibberellin binding |
C | 0016787 | molecular_function | hydrolase activity |
C | 0048444 | biological_process | floral organ morphogenesis |
D | 0005634 | cellular_component | nucleus |
D | 0005737 | cellular_component | cytoplasm |
D | 0009739 | biological_process | response to gibberellin |
D | 0009740 | biological_process | gibberellic acid mediated signaling pathway |
D | 0009939 | biological_process | positive regulation of gibberellic acid mediated signaling pathway |
D | 0010325 | biological_process | raffinose family oligosaccharide biosynthetic process |
D | 0010331 | molecular_function | gibberellin binding |
D | 0016787 | molecular_function | hydrolase activity |
D | 0048444 | biological_process | floral organ morphogenesis |
E | 0005634 | cellular_component | nucleus |
E | 0005737 | cellular_component | cytoplasm |
E | 0009739 | biological_process | response to gibberellin |
E | 0009740 | biological_process | gibberellic acid mediated signaling pathway |
E | 0009939 | biological_process | positive regulation of gibberellic acid mediated signaling pathway |
E | 0010325 | biological_process | raffinose family oligosaccharide biosynthetic process |
E | 0010331 | molecular_function | gibberellin binding |
E | 0016787 | molecular_function | hydrolase activity |
E | 0048444 | biological_process | floral organ morphogenesis |
F | 0005634 | cellular_component | nucleus |
F | 0005737 | cellular_component | cytoplasm |
F | 0009739 | biological_process | response to gibberellin |
F | 0009740 | biological_process | gibberellic acid mediated signaling pathway |
F | 0009939 | biological_process | positive regulation of gibberellic acid mediated signaling pathway |
F | 0010325 | biological_process | raffinose family oligosaccharide biosynthetic process |
F | 0010331 | molecular_function | gibberellin binding |
F | 0016787 | molecular_function | hydrolase activity |
F | 0048444 | biological_process | floral organ morphogenesis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE GA4 A 401 |
Chain | Residue |
A | ILE24 |
A | ARG251 |
A | TYR254 |
A | VAL326 |
A | GLY327 |
A | TYR329 |
A | HOH605 |
A | HOH607 |
A | PHE27 |
A | GLY122 |
A | SER123 |
A | ILE133 |
A | TYR134 |
A | ASP197 |
A | SER198 |
A | VAL246 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MPD A 501 |
Chain | Residue |
A | LEU23 |
A | LEU49 |
A | ASP50 |
A | ARG51 |
A | HOH640 |
B | MPD501 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NO3 A 601 |
Chain | Residue |
A | ARG35 |
A | HOH785 |
A | HOH848 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NO3 A 602 |
Chain | Residue |
A | THR231 |
A | ASP264 |
A | ARG265 |
A | HOH698 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NO3 A 603 |
Chain | Residue |
A | ARG51 |
A | LEU331 |
A | NO3604 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NO3 A 604 |
Chain | Residue |
A | HIS19 |
A | LEU23 |
A | ARG51 |
A | NO3603 |
B | ASN26 |
B | SER30 |
site_id | AC7 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE GA4 B 401 |
Chain | Residue |
B | ILE24 |
B | PHE27 |
B | GLY122 |
B | SER123 |
B | ILE133 |
B | TYR134 |
B | ASP197 |
B | SER198 |
B | ARG251 |
B | TYR254 |
B | VAL326 |
B | GLY327 |
B | TYR329 |
B | HOH702 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MPD B 501 |
Chain | Residue |
A | MPD501 |
B | LEU23 |
B | SER30 |
B | LEU49 |
B | ARG51 |
B | HOH719 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NO3 B 601 |
Chain | Residue |
B | ARG35 |
B | TRP253 |
B | HOH891 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NO3 B 602 |
Chain | Residue |
B | THR231 |
B | ASP264 |
B | ARG265 |
B | HOH789 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NO3 B 604 |
Chain | Residue |
A | ASN26 |
A | SER30 |
B | HIS19 |
B | LEU23 |
B | ARG51 |
B | PO4701 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 B 701 |
Chain | Residue |
B | ARG51 |
B | LEU330 |
B | LEU331 |
B | NO3604 |
B | HOH724 |
site_id | BC4 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE GA4 C 401 |
Chain | Residue |
C | PHE27 |
C | ARG35 |
C | GLY122 |
C | SER123 |
C | ILE133 |
C | TYR134 |
C | ASP197 |
C | SER198 |
C | VAL246 |
C | ARG251 |
C | TYR254 |
C | VAL326 |
C | GLY327 |
C | TYR329 |
C | HOH605 |
C | HOH607 |
site_id | BC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE MPD C 501 |
Chain | Residue |
D | ARG51 |
C | ASN26 |
C | SER30 |
C | LEU49 |
C | ASP50 |
C | ARG51 |
C | HOH638 |
D | ASN26 |
site_id | BC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE NO3 C 601 |
Chain | Residue |
C | ARG35 |
C | TRP253 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NO3 C 602 |
Chain | Residue |
C | THR231 |
C | ASP264 |
C | ARG265 |
C | HOH697 |
site_id | BC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NO3 C 603 |
Chain | Residue |
C | ARG51 |
C | LEU330 |
C | HOH642 |
site_id | BC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NO3 C 604 |
Chain | Residue |
C | ASN26 |
C | SER30 |
D | HIS19 |
D | LEU23 |
D | ARG51 |
site_id | CC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE GA4 D 401 |
Chain | Residue |
D | ILE24 |
D | PHE27 |
D | ARG35 |
D | GLY122 |
D | SER123 |
D | ILE133 |
D | TYR134 |
D | ASP197 |
D | SER198 |
D | ARG251 |
D | TYR254 |
D | VAL326 |
D | GLY327 |
D | TYR329 |
D | HOH604 |
D | HOH606 |
site_id | CC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MPD D 501 |
Chain | Residue |
D | LEU23 |
D | ASN26 |
D | LEU49 |
D | ASP50 |
D | ARG51 |
D | HOH630 |
site_id | CC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NO3 D 601 |
Chain | Residue |
D | ARG35 |
D | GLN249 |
D | TRP253 |
D | HOH704 |
site_id | CC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NO3 D 602 |
Chain | Residue |
D | THR231 |
D | ASP264 |
D | ARG265 |
D | HOH721 |
site_id | CC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE NO3 D 603 |
Chain | Residue |
D | ARG51 |
D | LEU331 |
site_id | CC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PO4 E 701 |
Chain | Residue |
E | ARG51 |
E | SER136 |
E | LEU330 |
site_id | CC7 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE GA4 E 401 |
Chain | Residue |
E | PHE27 |
E | ARG35 |
E | GLY122 |
E | SER123 |
E | ILE133 |
E | TYR134 |
E | ASP197 |
E | SER198 |
E | ARG251 |
E | TYR254 |
E | VAL326 |
E | GLY327 |
E | TYR329 |
E | HOH702 |
E | HOH730 |
site_id | CC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MPD E 501 |
Chain | Residue |
E | ASN26 |
E | SER30 |
E | LEU49 |
E | ARG51 |
E | HOH711 |
F | MPD501 |
site_id | CC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NO3 E 601 |
Chain | Residue |
E | ARG35 |
E | GLN249 |
E | TRP253 |
E | HOH796 |
site_id | DC1 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE GA4 F 401 |
Chain | Residue |
F | PHE27 |
F | GLY122 |
F | SER123 |
F | ILE133 |
F | TYR134 |
F | ASP197 |
F | SER198 |
F | PHE245 |
F | ARG251 |
F | TYR254 |
F | VAL326 |
F | GLY327 |
F | TYR329 |
F | HOH604 |
F | HOH625 |
site_id | DC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MPD F 501 |
Chain | Residue |
E | MPD501 |
F | LEU23 |
F | SER30 |
F | LEU49 |
F | ARG51 |
F | HOH626 |
site_id | DC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE NO3 F 601 |
Chain | Residue |
F | ARG35 |
F | HOH752 |
site_id | DC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NO3 F 602 |
Chain | Residue |
F | THR231 |
F | ASP264 |
F | ARG265 |
site_id | DC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NO3 F 603 |
Chain | Residue |
F | LEU330 |
F | LEU331 |
F | HOH631 |
Functional Information from PROSITE/UniProt
site_id | PS01173 |
Number of Residues | 17 |
Details | LIPASE_GDXG_HIS Lipolytic enzymes "G-D-X-G" family, putative histidine active site. IIfFHGGSFvhsSasST |
Chain | Residue | Details |
A | ILE116-THR132 |
site_id | PS01174 |
Number of Residues | 13 |
Details | LIPASE_GDXG_SER Lipolytic enzymes "G-D-X-G" family, putative serine active site. VfLSGDSSGGnIA |
Chain | Residue | Details |
A | VAL192-ALA204 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10038 |
Chain | Residue | Details |
A | SER198 | |
B | SER198 | |
C | SER198 | |
D | SER198 | |
E | SER198 | |
F | SER198 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | ACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:Q5NUF3 |
Chain | Residue | Details |
A | ASP296 | |
B | ASP296 | |
C | ASP296 | |
D | ASP296 | |
E | ASP296 | |
F | ASP296 |
site_id | SWS_FT_FI3 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000269|PubMed:19037316, ECO:0007744|PDB:3EBL |
Chain | Residue | Details |
A | GLY122 | |
C | TYR134 | |
C | SER198 | |
C | GLY327 | |
D | GLY122 | |
D | TYR134 | |
D | SER198 | |
D | GLY327 | |
E | GLY122 | |
E | TYR134 | |
E | SER198 | |
A | TYR134 | |
E | GLY327 | |
F | GLY122 | |
F | TYR134 | |
F | SER198 | |
F | GLY327 | |
A | SER198 | |
A | GLY327 | |
B | GLY122 | |
B | TYR134 | |
B | SER198 | |
B | GLY327 | |
C | GLY122 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:19037316, ECO:0007744|PDB:3ED1 |
Chain | Residue | Details |
A | ASP250 | |
B | ASP250 | |
C | ASP250 | |
D | ASP250 | |
E | ASP250 | |
F | ASP250 |