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2GCP

Crystal structure of the human RhoC-GSP complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000281biological_processmitotic cytokinesis
A0003924molecular_functionGTPase activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005634cellular_componentnucleus
A0005789cellular_componentendoplasmic reticulum membrane
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0007015biological_processactin filament organization
A0007165biological_processsignal transduction
A0007264biological_processsmall GTPase-mediated signal transduction
A0016020cellular_componentmembrane
A0019901molecular_functionprotein kinase binding
A0030335biological_processpositive regulation of cell migration
A0031334biological_processpositive regulation of protein-containing complex assembly
A0032154cellular_componentcleavage furrow
A0032420cellular_componentstereocilium
A0032956biological_processregulation of actin cytoskeleton organization
A0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
A0043297biological_processapical junction assembly
A0044319biological_processwound healing, spreading of cells
A0051496biological_processpositive regulation of stress fiber assembly
A0060193biological_processpositive regulation of lipase activity
A0070062cellular_componentextracellular exosome
A1902766biological_processskeletal muscle satellite cell migration
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 2001
ChainResidue
ATHR19
ATHR37
AGSP1001
AHOH3025
AHOH3036

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 2002
ChainResidue
AHOH3091
AHIS105
AARG122
AHOH3089
AHOH3090

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG A 2003
ChainResidue
AARG145
ATYR156

site_idAC4
Number of Residues28
DetailsBINDING SITE FOR RESIDUE GSP A 1001
ChainResidue
AGLY14
AALA15
ACYS16
AGLY17
ALYS18
ATHR19
ACYS20
APHE30
ATYR34
ATHR37
AGLY62
ALYS118
AASP120
APHE154
ASER160
AALA161
ALYS162
AMG2001
AEDO3002
AHOH3015
AHOH3022
AHOH3025
AHOH3036
AHOH3077
AHOH3099
AHOH3100
AHOH3103
AHOH3104

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 3001
ChainResidue
AASP13
AGLY14
AASP49
ASER88
AASP90
ASER91

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE EDO A 3002
ChainResidue
ATHR19
ACYS20
AVAL33
ATYR34
AVAL35
AGSP1001
AHOH3025
AHOH3083
AHOH3103
AHOH3124

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLY12
AASP59
AASN117

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: ADP-ribosylasparagine; by botulinum toxin => ECO:0000250
ChainResidueDetails
AASN41

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: O-linked (GlcNAc) tyrosine; by Photorhabdus PAU_02230 => ECO:0000269|PubMed:24141704
ChainResidueDetails
ATYR34

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: (Microbial infection) O-linked (Glc) threonine; by C.difficile toxins TcdA and TcdB => ECO:0000269|PubMed:24905543
ChainResidueDetails
ATHR37

218853

건을2024-04-24부터공개중

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