7XOP

Cryo-EM structure of occupied ring subunit 1 (OR1) of GroEL from GroEL-UGT1A double occupied ring complex

Functional Information from GO Data

Chain	GOid	namespace	contents
K	0000287	molecular_function	magnesium ion binding
K	0005515	molecular_function	protein binding
K	0005524	molecular_function	ATP binding
K	0005737	cellular_component	cytoplasm
K	0005829	cellular_component	cytosol
K	0006457	biological_process	protein folding
K	0009314	biological_process	response to radiation
K	0009408	biological_process	response to heat
K	0016020	cellular_component	membrane
K	0016853	molecular_function	isomerase activity
K	0016887	molecular_function	ATP hydrolysis activity
K	0019068	biological_process	virion assembly
K	0042026	biological_process	protein refolding
K	0042802	molecular_function	identical protein binding
K	0051082	molecular_function	unfolded protein binding
K	0051085	biological_process	chaperone cofactor-dependent protein refolding
K	0140662	molecular_function	ATP-dependent protein folding chaperone
K	1990220	cellular_component	GroEL-GroES complex

Functional Information from PROSITE/UniProt

site_id	PS00296
Number of Residues	12
Details	CHAPERONINS_CPN60 Chaperonins cpn60 signature. AAVEEGVVaGGG

Chain	Residue	Details
K	ALA405-GLY416

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00600, ECO:0000269|PubMed:25174333, ECO:0000305|PubMed:14517228, ECO:0000305|PubMed:9285585, ECO:0007744|PDB:1AON, ECO:0007744|PDB:1PCQ, ECO:0007744|PDB:1PF9, ECO:0007744|PDB:3WVL

Chain	Residue	Details
K	THR30
K	ASP87
K	GLY415
K	ASN479
K	ASP495

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site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00600, ECO:0000269|PubMed:25174333, ECO:0000305|PubMed:14517228, ECO:0000305|PubMed:9285585, ECO:0007744|PDB:1AON, ECO:0007744|PDB:1PF9, ECO:0007744|PDB:3WVL

Chain	Residue	Details
K	LYS51

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site_id	SWS_FT_FI3
Number of Residues	5
Details	MOD_RES: N6-succinyllysine => ECO:0000269|PubMed:21151122

Chain	Residue	Details
K	LYS34
K	LYS51
K	LYS277
K	LYS321
K	LYS390

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122

Chain	Residue	Details
K	LYS117

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