5L95

Crystal structure of human UBA5 in complex with UFM1 and AMP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008641	molecular_function	ubiquitin-like modifier activating enzyme activity
B	0008641	molecular_function	ubiquitin-like modifier activating enzyme activity
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005783	cellular_component	endoplasmic reticulum
C	0007420	biological_process	brain development
C	0033146	biological_process	regulation of intracellular estrogen receptor signaling pathway
C	0034976	biological_process	response to endoplasmic reticulum stress
C	0042308	biological_process	negative regulation of protein import into nucleus
C	0043066	biological_process	negative regulation of apoptotic process
C	0061709	biological_process	reticulophagy
C	0071569	biological_process	protein ufmylation
C	1990592	biological_process	protein K69-linked ufmylation
D	0005515	molecular_function	protein binding
D	0005634	cellular_component	nucleus
D	0005737	cellular_component	cytoplasm
D	0005783	cellular_component	endoplasmic reticulum
D	0007420	biological_process	brain development
D	0033146	biological_process	regulation of intracellular estrogen receptor signaling pathway
D	0034976	biological_process	response to endoplasmic reticulum stress
D	0042308	biological_process	negative regulation of protein import into nucleus
D	0043066	biological_process	negative regulation of apoptotic process
D	0061709	biological_process	reticulophagy
D	0071569	biological_process	protein ufmylation
D	1990592	biological_process	protein K69-linked ufmylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	21
Details	binding site for residue AMP A 401

Chain	Residue
A	GLY80
A	ILE151
A	THR152
A	CYS181
A	VAL182
A	ASP183
A	ASN184
A	ALA187
A	HOH529
A	HOH534
A	HOH566
A	GLY82
C	VAL82
C	GLY83
A	GLY83
A	ASP104
A	TYR105
A	ASP106
A	LYS127
A	TYR149
A	ASN150

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site_id	AC2
Number of Residues	4
Details	binding site for residue ZN A 402

Chain	Residue
A	CYS226
A	CYS229
A	CYS303
A	CYS308

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site_id	AC3
Number of Residues	4
Details	binding site for residue ZN B 401

Chain	Residue
B	CYS226
B	CYS229
B	CYS303
B	CYS308

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Functional Information from PROSITE/UniProt

site_id	PS00065
Number of Residues	29
Details	D_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. VAIVGvGGVGsvtaemltrcgigkLLlFD

Chain	Residue	Details
A	VAL76-ASP104

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1) => ECO:0000269|PubMed:25219498

Chain	Residue	Details
C	LYS69
D	LYS69

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site_id	SWS_FT_FI2
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) => ECO:0000269|PubMed:15071506, ECO:0000269|PubMed:25219498, ECO:0000269|PubMed:27653677

Chain	Residue	Details
A	GLY83
C	GLY83
A	ASN150
D	GLY83
B	GLY83
B	LYS127
B	ASN150
B	ASN184

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site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:20368332, ECO:0000269|PubMed:27653677, ECO:0000269|PubMed:30412706, ECO:0007744|PDB:5L95, ECO:0007744|PDB:6H78

Chain	Residue	Details
A	ASP104
B	ASP104

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site_id	SWS_FT_FI4
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:20368332, ECO:0000269|PubMed:27653677, ECO:0000269|PubMed:30412706, ECO:0007744|PDB:5IAA, ECO:0007744|PDB:5L95, ECO:0007744|PDB:6H77, ECO:0007744|PDB:6H78

Chain	Residue	Details
A	CYS226
A	CYS229
A	CYS303
A	CYS308
B	CYS226
B	CYS229
B	CYS303
B	CYS308

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