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5YEW

Structural basis for GTP hydrolysis and conformational change of mitofusin 1 in mediating mitochondrial fusion

Functional Information from GO Data
ChainGOidnamespacecontents
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
A0005741cellular_componentmitochondrial outer membrane
A0008053biological_processmitochondrial fusion
A0016020cellular_componentmembrane
B0003924molecular_functionGTPase activity
B0005525molecular_functionGTP binding
B0005741cellular_componentmitochondrial outer membrane
B0008053biological_processmitochondrial fusion
B0016020cellular_componentmembrane
C0003924molecular_functionGTPase activity
C0005525molecular_functionGTP binding
C0005741cellular_componentmitochondrial outer membrane
C0008053biological_processmitochondrial fusion
C0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues19
Detailsbinding site for residue GDP A 801
ChainResidue
ASER85
AASN237
AARG238
AASP240
ASER284
AALA285
ALYS286
ABEF802
AK803
AMG804
BGLU245
AGLY87
ALYS88
ASER89
ASER90
ASER103
AGLY104
AILE105
ATHR109

site_idAC2
Number of Residues9
Detailsbinding site for residue BEF A 802
ChainResidue
ATHR84
AGLY106
AHIS107
AILE108
ATHR109
AGLY181
AGDP801
AK803
AMG804

site_idAC3
Number of Residues5
Detailsbinding site for residue K A 803
ChainResidue
ASER85
AGLY104
AGLY106
AGDP801
ABEF802

site_idAC4
Number of Residues5
Detailsbinding site for residue MG A 804
ChainResidue
ASER89
ATHR109
AASP178
AGDP801
ABEF802

site_idAC5
Number of Residues20
Detailsbinding site for residue GDP B 801
ChainResidue
AGLU245
BARG83
BSER85
BSER86
BGLY87
BLYS88
BSER89
BSER90
BSER103
BGLY104
BTHR109
BASN237
BARG238
BASP240
BSER284
BALA285
BLYS286
BBEF802
BK803
BMG804

site_idAC6
Number of Residues9
Detailsbinding site for residue BEF B 802
ChainResidue
BTHR84
BLYS88
BGLY106
BHIS107
BILE108
BTHR109
BGLY181
BGDP801
BK803

site_idAC7
Number of Residues5
Detailsbinding site for residue K B 803
ChainResidue
BSER85
BGLY104
BGLY106
BGDP801
BBEF802

site_idAC8
Number of Residues3
Detailsbinding site for residue MG B 804
ChainResidue
BSER89
BTHR109
BGDP801

site_idAC9
Number of Residues19
Detailsbinding site for residue GDP C 801
ChainResidue
CSER85
CSER86
CGLY87
CLYS88
CSER89
CSER90
CSER103
CGLY104
CILE105
CASN237
CARG238
CASP240
CGLU245
CSER284
CALA285
CLYS286
CBEF802
CK803
CMG804

site_idAD1
Number of Residues10
Detailsbinding site for residue BEF C 802
ChainResidue
CPRO180
CGLY181
CGDP801
CK803
CMG804
CTHR84
CLYS88
CHIS107
CILE108
CTHR109

site_idAD2
Number of Residues5
Detailsbinding site for residue K C 803
ChainResidue
CSER85
CGLY104
CGLY106
CGDP801
CBEF802

site_idAD3
Number of Residues4
Detailsbinding site for residue MG C 804
ChainResidue
CSER89
CTHR109
CGDP801
CBEF802

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:27920125, ECO:0000269|PubMed:28114303, ECO:0007744|PDB:5GNR, ECO:0007744|PDB:5GNS, ECO:0007744|PDB:5GOE, ECO:0007744|PDB:5GOF
ChainResidueDetails
BSER85
CSER85

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:27920125, ECO:0000269|PubMed:28114303, ECO:0007744|PDB:5GNS, ECO:0007744|PDB:5GOE, ECO:0007744|PDB:5GOF
ChainResidueDetails
BASN237
CASN237

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:27920125, ECO:0000269|PubMed:28114303, ECO:0007744|PDB:5GNR, ECO:0007744|PDB:5GOE, ECO:0007744|PDB:5GOF
ChainResidueDetails
BSER284
CSER284

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:27920125, ECO:0007744|PDB:5GNS
ChainResidueDetails
BLYS286
CLYS286

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PDB entries from 2024-09-11

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