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2GCN

Crystal structure of the human RhoC-GDP 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 Residues6
DetailsBINDING SITE FOR RESIDUE MG A 2001
ChainResidue
ATHR19
ATHR37
AGDP1001
AHOH3143
AHOH3144
AHOH3145

site_idAC2
Number of Residues24
DetailsBINDING SITE FOR RESIDUE GDP A 1001
ChainResidue
ALYS18
ATHR19
ACYS20
APHE30
AVAL35
ALYS118
AASP120
ALEU121
ASER160
AALA161
ALYS162
AMG2001
AHOH3011
AHOH3046
AHOH3049
AHOH3059
AHOH3079
AHOH3143
AHOH3144
AHOH3145
AHOH3197
AALA15
ACYS16
AGLY17

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 3001
ChainResidue
APHE154
ATHR163
AGLU165
AHOH3073

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 3002
ChainResidue
AARG122
AALA177
AGLY178
ALEU179
AEDO3003
AHOH3102
AHOH3117
AHOH3118
AHOH3125

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 3003
ChainResidue
AARG176
ALEU179
AEDO3002
AHOH3051
AHOH3179

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 3004
ChainResidue
AGLY62
AASP67
AARG70
ALYS98
ATRP99
AHOH3044
AHOH3122
AHOH3163
AHOH3188

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 3005
ChainResidue
AILE43
AASP45
AASP90

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

PDB entries from 2024-04-24

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