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5D3Q

Dynamin 1 GTPase-BSE fusion dimer complexed with GDP

Functional Information from GO Data
ChainGOidnamespacecontents
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
B0003924molecular_functionGTPase activity
B0005525molecular_functionGTP binding
Functional Information from PDB Data
site_idAC1
Number of Residues22
Detailsbinding site for residue GDP A 801
ChainResidue
ASER41
ALEU209
AVAL235
AASN236
AARG237
ASER238
AGLN239
AILE242
AEDO802
AHOH912
AHOH964
AALA42
AHOH1099
BASP211
BHOH974
AGLY43
ALYS44
ASER45
ASER46
AARG59
ALYS206
AASP208

site_idAC2
Number of Residues5
Detailsbinding site for residue EDO A 802
ChainResidue
ASER45
APRO58
AARG59
AGDP801
AHOH1009

site_idAC3
Number of Residues22
Detailsbinding site for residue GDP B 801
ChainResidue
AASP211
AHOH987
BSER41
BALA42
BGLY43
BLYS44
BSER45
BSER46
BARG59
BLYS206
BASP208
BLEU209
BVAL235
BASN236
BARG237
BSER238
BGLN239
BHOH916
BHOH1009
BHOH1073
BHOH1077
BHOH1102

site_idAC4
Number of Residues5
Detailsbinding site for residue EDO B 802
ChainResidue
BLEU207
BASP208
BMET210
BHIS262
BHOH940

Functional Information from PROSITE/UniProt
site_idPS00410
Number of Residues10
DetailsG_DYNAMIN_1 Dynamin-type guanine nucleotide-binding (G) domain signature. LPRGSGIVTR
ChainResidueDetails
ALEU57-ARG66

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:20428113, ECO:0000269|PubMed:26612256, ECO:0007744|PDB:5D3Q
ChainResidueDetails
BSER41
ASER41

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:20428113, ECO:0000269|PubMed:26612256, ECO:0007744|PDB:2X2E, ECO:0007744|PDB:2X2F, ECO:0007744|PDB:5D3Q
ChainResidueDetails
ALYS206
AASP208
BGLY43
BSER45
BLYS206
BASP208
AGLY43
ASER45

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:20428113, ECO:0000269|PubMed:26612256, ECO:0000269|PubMed:30069048, ECO:0007744|PDB:2X2E, ECO:0007744|PDB:2X2F, ECO:0007744|PDB:5D3Q, ECO:0007744|PDB:6DLU
ChainResidueDetails
BGLN239
AASN236
AARG237
AGLN239
BLYS44
BSER46
BASN236
BARG237
ALYS44
ASER46

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:26612256, ECO:0007744|PDB:5D3Q
ChainResidueDetails
AARG59
BARG59

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:20428113, ECO:0007744|PDB:2X2E, ECO:0007744|PDB:2X2F
ChainResidueDetails
AGLY60
BGLY60

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:20428113, ECO:0000269|PubMed:26612256, ECO:0000269|PubMed:30069048, ECO:0007744|PDB:2X2E, ECO:0007744|PDB:5D3Q, ECO:0007744|PDB:6DLU
ChainResidueDetails
AASP211
BASP211

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P39053
ChainResidueDetails
ATYR80
BTYR80

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; alternate => ECO:0000250|UniProtKB:P39053
ChainResidueDetails
ATYR125
BTYR125

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P39053
ChainResidueDetails
ASER306
BSER306

219869

PDB entries from 2024-05-15

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