3C5C
Crystal structure of human Ras-like, family 12 protein in complex with GDP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003924 | molecular_function | GTPase activity |
A | 0005525 | molecular_function | GTP binding |
A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0003924 | molecular_function | GTPase activity |
B | 0005525 | molecular_function | GTP binding |
B | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
C | 0003924 | molecular_function | GTPase activity |
C | 0005525 | molecular_function | GTP binding |
C | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
D | 0003924 | molecular_function | GTPase activity |
D | 0005525 | molecular_function | GTP binding |
D | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 202 |
Chain | Residue |
A | SER34 |
A | GDP201 |
A | HOH301 |
A | HOH302 |
A | HOH303 |
A | HOH304 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG A 203 |
Chain | Residue |
A | HOH359 |
A | ASP55 |
A | HOH352 |
A | HOH355 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 202 |
Chain | Residue |
B | SER34 |
B | GDP201 |
B | HOH301 |
B | HOH302 |
B | HOH303 |
B | HOH304 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG B 203 |
Chain | Residue |
B | ASP55 |
B | HOH370 |
B | HOH371 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG C 202 |
Chain | Residue |
C | SER34 |
C | GDP201 |
C | HOH301 |
C | HOH302 |
C | HOH303 |
C | HOH304 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MG C 203 |
Chain | Residue |
C | ASP55 |
C | HOH352 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG D 202 |
Chain | Residue |
D | SER34 |
D | GDP201 |
D | HOH301 |
D | HOH302 |
D | HOH303 |
D | HOH304 |
site_id | AC8 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE GDP A 201 |
Chain | Residue |
A | ARG29 |
A | GLY30 |
A | ALA31 |
A | GLY32 |
A | LYS33 |
A | SER34 |
A | ALA35 |
A | SER47 |
A | ASN134 |
A | LYS135 |
A | ASP137 |
A | MET138 |
A | SER164 |
A | ALA165 |
A | CYS166 |
A | MG202 |
A | HOH301 |
A | HOH303 |
A | HOH304 |
A | HOH308 |
A | HOH317 |
A | HOH326 |
A | HOH353 |
B | ASN89 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE UNX A 204 |
Chain | Residue |
A | ARG142 |
A | THR145 |
A | LYS146 |
site_id | BC1 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE GDP B 201 |
Chain | Residue |
B | ARG28 |
B | GLY30 |
B | ALA31 |
B | GLY32 |
B | LYS33 |
B | SER34 |
B | ALA35 |
B | SER47 |
B | ASN134 |
B | LYS135 |
B | ASP137 |
B | MET138 |
B | SER164 |
B | ALA165 |
B | CYS166 |
B | MG202 |
B | HOH301 |
B | HOH304 |
B | HOH311 |
B | HOH312 |
B | HOH333 |
B | HOH367 |
site_id | BC2 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE GDP C 201 |
Chain | Residue |
C | HOH304 |
C | HOH307 |
C | HOH313 |
C | HOH326 |
C | HOH329 |
C | HOH334 |
D | ASN89 |
C | ARG29 |
C | GLY30 |
C | ALA31 |
C | GLY32 |
C | LYS33 |
C | SER34 |
C | ALA35 |
C | SER47 |
C | ASN134 |
C | LYS135 |
C | ASP137 |
C | MET138 |
C | SER164 |
C | ALA165 |
C | CYS166 |
C | MG202 |
C | HOH301 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE UNX C 204 |
Chain | Residue |
C | ARG44 |
C | PHE45 |
D | HOH340 |
site_id | BC4 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE GDP D 201 |
Chain | Residue |
B | ARG44 |
D | ARG28 |
D | ARG29 |
D | GLY30 |
D | ALA31 |
D | GLY32 |
D | LYS33 |
D | SER34 |
D | ALA35 |
D | PHE45 |
D | SER47 |
D | ASN134 |
D | LYS135 |
D | ASP137 |
D | MET138 |
D | SER164 |
D | ALA165 |
D | CYS166 |
D | MG202 |
D | HOH301 |
D | HOH303 |
D | HOH304 |
D | HOH314 |
D | HOH319 |
site_id | BC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE UNX D 203 |
Chain | Residue |
D | ASP55 |
D | PHE156 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | BINDING: |
Chain | Residue | Details |
A | GLY27 | |
A | ASN134 | |
B | GLY27 | |
B | ASN134 | |
C | GLY27 | |
C | ASN134 | |
D | GLY27 | |
D | ASN134 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | ASP74 | |
B | ASP74 | |
C | ASP74 | |
D | ASP74 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ksj |
Chain | Residue | Details |
B | LEU78 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ksj |
Chain | Residue | Details |
C | LEU78 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ksj |
Chain | Residue | Details |
D | LEU78 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ksj |
Chain | Residue | Details |
A | GLY30 |
site_id | CSA5 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ksj |
Chain | Residue | Details |
B | GLY30 |