4P22

Crystal Structure of N-terminal Fragments of E1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008641	molecular_function	ubiquitin-like modifier activating enzyme activity
A	0036211	biological_process	protein modification process
B	0008641	molecular_function	ubiquitin-like modifier activating enzyme activity
B	0036211	biological_process	protein modification process

Functional Information from PROSITE/UniProt

site_id	PS00536
Number of Residues	9
Details	UBIQUITIN_ACTIVAT_1 Ubiquitin-activating enzyme signature 1. KACSGKFmP

Chain	Residue	Details
A	LYS411-PRO419

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	MOD_RES: N-acetylserine => ECO:0007744|PubMed:22814378

Chain	Residue	Details
A	SER2
B	SER2

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site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:9099746

Chain	Residue	Details
A	SER4
B	SER4

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site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648

Chain	Residue	Details
A	SER13
B	SER13

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site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q02053

Chain	Residue	Details
A	SER21
A	SER24
B	SER21
B	SER24

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site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER46
B	SER46

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site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q02053

Chain	Residue	Details
A	TYR55
B	TYR55

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