8EOJ

Microsomal triglyceride transfer protein

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003756	molecular_function	protein disulfide isomerase activity
B	0005319	molecular_function	lipid transporter activity
B	0005548	molecular_function	phospholipid transporter activity
B	0006869	biological_process	lipid transport
B	0008289	molecular_function	lipid binding

Functional Information from PROSITE/UniProt

site_id	PS00014
Number of Residues	4
Details	ER_TARGET Endoplasmic reticulum targeting sequence. KDEL

Chain	Residue	Details
A	LYS505-LEU508

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site_id	PS00194
Number of Residues	19
Details	THIOREDOXIN_1 Thioredoxin family active site. LVeFYapWCGHCKaLapeY

Chain	Residue	Details
A	LEU45-TYR63
A	PHE389-TRP407

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Nucleophile

Chain	Residue	Details
A	CYS53
A	CYS56

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Nucleophile => ECO:0000250

Chain	Residue	Details
A	CYS397
A	CYS400

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site_id	SWS_FT_FI3
Number of Residues	2
Details	SITE: Contributes to redox potential value

Chain	Residue	Details
A	GLY54
A	HIS55

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site_id	SWS_FT_FI4
Number of Residues	1
Details	SITE: Lowers pKa of C-terminal Cys of first active site

Chain	Residue	Details
A	ARG120

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site_id	SWS_FT_FI5
Number of Residues	2
Details	SITE: Contributes to redox potential value => ECO:0000250

Chain	Residue	Details
A	GLY398
A	HIS399

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site_id	SWS_FT_FI6
Number of Residues	1
Details	SITE: Lowers pKa of C-terminal Cys of second active site => ECO:0000250

Chain	Residue	Details
A	ARG461

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site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P09103

Chain	Residue	Details
A	LYS200

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site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P09103

Chain	Residue	Details
A	LYS222
A	LYS271

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site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:32149426

Chain	Residue	Details
A	SER331
A	SER427

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site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039, ECO:0000269|PubMed:32149426

Chain	Residue	Details
A	SER357

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 191

Chain	Residue	Details
A	CYS53	nucleofuge, nucleophile, proton acceptor, proton donor
A	GLY54	activator, modifies pKa
A	HIS55	modifies pKa, proton acceptor, proton donor
A	CYS56

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