2E1R

Structure of eEF2 in complex with a sordarin derivative

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003746	molecular_function	translation elongation factor activity
A	0003924	molecular_function	GTPase activity
A	0005515	molecular_function	protein binding
A	0005525	molecular_function	GTP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006412	biological_process	translation
A	0006414	biological_process	translational elongation
A	0016787	molecular_function	hydrolase activity
A	0019843	molecular_function	rRNA binding
A	0042802	molecular_function	identical protein binding
A	0043022	molecular_function	ribosome binding
A	0045901	biological_process	positive regulation of translational elongation
A	0051087	molecular_function	protein-folding chaperone binding
A	1990145	biological_process	maintenance of translational fidelity
A	1990904	cellular_component	ribonucleoprotein complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE SOD A 901

Chain	Residue
A	PRO487
A	PRO727
A	VAL774
A	TRP801
A	GLN490
A	LEU519
A	TYR521
A	SER523
A	GLU524
A	ILE529
A	VAL561
A	ALA562

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site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE GDP A 902

Chain	Residue
A	VAL28
A	HIS30
A	GLY31
A	LYS32
A	SER33
A	THR34
A	ASN158
A	LYS159
A	ASP161
A	SER213
A	GLY214
A	LEU215

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Functional Information from PROSITE/UniProt

site_id	PS00301
Number of Residues	16
Details	G_TR_1 Translational (tr)-type guanine nucleotide-binding (G) domain signature. DTrkdEQeRGITIksT

Chain	Residue	Details
A	ASP58-THR73

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: BINDING => ECO:0000305|PubMed:15316019, ECO:0000305|PubMed:17082187, ECO:0007744|PDB:1U2R, ECO:0007744|PDB:2NPF

Chain	Residue	Details
A	ALA26

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000305|PubMed:15316019, ECO:0000305|PubMed:17082187, ECO:0007744|PDB:1U2R, ECO:0007744|PDB:2E1R, ECO:0007744|PDB:2NPF

Chain	Residue	Details
A	ASN158
A	SER213

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: N6-methyllysine; by EFM3; alternate => ECO:0000269|PubMed:24517342, ECO:0000269|PubMed:25086354

Chain	Residue	Details
A	LYS509

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198

Chain	Residue	Details
A	SER579

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: N6-methyllysine; by EFM2; alternate => ECO:0000269|PubMed:24517342, ECO:0000269|PubMed:25086354

Chain	Residue	Details
A	LYS613

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Diphthamide => ECO:0000269|PubMed:15316019, ECO:0000269|PubMed:16950777, ECO:0000269|PubMed:721806

Chain	Residue	Details
A	HIS699

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site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19779198

Chain	Residue	Details
A	THR713
A	THR763

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site_id	SWS_FT_FI8
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047

Chain	Residue	Details
A	LYS841

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1ksj

Chain	Residue	Details
A	ASP29

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site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1ksj

Chain	Residue	Details
A	HIS108

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