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3AB3

Crystal structure of p115RhoGEF RGS domain in complex with G alpha 13

Functional Information from GO Data
ChainGOidnamespacecontents
A0001664molecular_functionG protein-coupled receptor binding
A0003924molecular_functionGTPase activity
A0007165biological_processsignal transduction
A0007186biological_processG protein-coupled receptor signaling pathway
A0007266biological_processRho protein signal transduction
A0019001molecular_functionguanyl nucleotide binding
A0031683molecular_functionG-protein beta/gamma-subunit complex binding
B0005085molecular_functionguanyl-nucleotide exchange factor activity
B0005737cellular_componentcytoplasm
C0001664molecular_functionG protein-coupled receptor binding
C0003924molecular_functionGTPase activity
C0007165biological_processsignal transduction
C0007186biological_processG protein-coupled receptor signaling pathway
C0007266biological_processRho protein signal transduction
C0019001molecular_functionguanyl nucleotide binding
C0031683molecular_functionG-protein beta/gamma-subunit complex binding
D0005085molecular_functionguanyl-nucleotide exchange factor activity
D0005737cellular_componentcytoplasm
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 501
ChainResidue
ASER62
ATHR203
AGDP401
AHOH408
AHOH409
AALF601

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE GDP A 401
ChainResidue
ALYS61
ASER62
ATHR63
ASER173
ALEU197
ALEU198
AARG200
AASN291
ALYS292
AASP294
ALEU295
ATHR348
AALA349
AILE350
AHOH381
AHOH408
AMG501
AALF601
AGLU58
ASER59
AGLY60

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ALF A 601
ChainResidue
AGLY57
AGLU58
ALYS61
AARG200
APRO202
ATHR203
AVAL223
AGLY224
AGLY225
AGLN226
AGDP401
AHOH408
AHOH409
AMG501

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG C 502
ChainResidue
CHOH1
CSER62
CTHR203
CASP222
CHOH388
CGDP402
CALF602

site_idAC5
Number of Residues20
DetailsBINDING SITE FOR RESIDUE GDP C 402
ChainResidue
CHOH1
CGLU58
CSER59
CGLY60
CLYS61
CSER62
CTHR63
CSER173
CLEU197
CLEU198
CARG200
CASN291
CLYS292
CASP294
CLEU295
CTHR348
CALA349
CILE350
CMG502
CALF602

site_idAC6
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ALF C 602
ChainResidue
CHOH1
CGLY57
CGLU58
CLYS61
CARG200
CPRO202
CTHR203
CVAL223
CGLY224
CGLY225
CGLN226
CHOH388
CGDP402
CMG502

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsLIPID: N-myristoyl glycine => ECO:0000250|UniProtKB:P08754
ChainResidueDetails
AGLY17
CGLY17

site_idSWS_FT_FI2
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q14344
ChainResidueDetails
ACYS18
CCYS18

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:16388592, ECO:0000269|PubMed:18940608, ECO:0007744|PDB:1ZCB, ECO:0007744|PDB:3CX6, ECO:0007744|PDB:3CX7
ChainResidueDetails
AGLU58
ALEU197
AASN291
AALA349
CGLU58
CLEU197
CASN291
CALA349

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:18940608, ECO:0007744|PDB:3CX6
ChainResidueDetails
ASER62
ATHR203
CSER62
CTHR203

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:18940608, ECO:0007744|PDB:3CX7
ChainResidueDetails
ASER173
CSER173

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q14344
ChainResidueDetails
ATHR203
CTHR203

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PDB entries from 2024-07-24

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