5WGB

Crystal Structure of the Human mitochondrial Cysteine Desulfurase in complex with ISD11 and E. coli ACP1 protein at 2.75A

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0030170	molecular_function	pyridoxal phosphate binding
A	0031071	molecular_function	cysteine desulfurase activity
A	0044571	biological_process	[2Fe-2S] cluster assembly
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0016226	biological_process	iron-sulfur cluster assembly
B	0016604	cellular_component	nuclear body
B	0042803	molecular_function	protein homodimerization activity
B	0044571	biological_process	[2Fe-2S] cluster assembly
B	0044572	biological_process	[4Fe-4S] cluster assembly
B	0099128	cellular_component	mitochondrial [2Fe-2S] assembly complex
B	1990221	cellular_component	L-cysteine desulfurase complex
B	1990229	cellular_component	iron-sulfur cluster assembly complex
C	0000035	molecular_function	acyl binding
C	0000036	molecular_function	acyl carrier activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006633	biological_process	fatty acid biosynthetic process
C	0009245	biological_process	lipid A biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	binding site for residue PLP A 501

Chain	Residue
A	GLY126
A	LYS258
A	LYS263
A	ALA127
A	THR128
A	HIS156
A	ASP232
A	ALA234
A	GLN235
A	SER255
A	HIS257

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site_id	AC2
Number of Residues	10
Details	binding site for residue 8Q1 C 301

Chain	Residue
B	TYR31
B	ILE36
B	ALA39
B	PHE40
B	ASN43
B	LYS44
B	ILE52
B	LEU55
B	ASP62
C	SER36

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Functional Information from PROSITE/UniProt

site_id	PS00012
Number of Residues	16
Details	PHOSPHOPANTETHEINE Phosphopantetheine attachment site. DLGADSLDTVELVMAL

Chain	Residue	Details
C	ASP31-LEU46

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site_id	PS00595
Number of Residues	20
Details	AA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. IDLMsiSGHKiygpk.GvGaI

Chain	Residue	Details
A	ILE249-ILE268

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	MOD_RES: O-(pantetheine 4'-phosphoryl)serine => ECO:0000255|PROSITE-ProRule:PRU00258

Chain	Residue	Details
C	SER36
B	LYS44

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q8K215

Chain	Residue	Details
B	LYS47

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site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:29097656, ECO:0000269|PubMed:31101807, ECO:0000269|PubMed:34824239, ECO:0007744|PDB:5WKP, ECO:0007744|PDB:5WLW, ECO:0007744|PDB:6NZU, ECO:0007744|PDB:6UXE, ECO:0007744|PDB:6W1D, ECO:0007744|PDB:6WI2, ECO:0007744|PDB:6WIH, ECO:0007744|PDB:7RTK

Chain	Residue	Details
A	THR128
A	GLN235
A	SER255
A	HIS257

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:29097656, ECO:0000269|PubMed:31101807, ECO:0007744|PDB:5WKP, ECO:0007744|PDB:5WLW, ECO:0007744|PDB:6NZU

Chain	Residue	Details
A	THR295

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site_id	SWS_FT_FI5
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:29097656, ECO:0007744|PDB:5WLW

Chain	Residue	Details
A	CYS381

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:29097656, ECO:0000269|PubMed:31101807, ECO:0000269|PubMed:34824239, ECO:0007744|PDB:5WKP, ECO:0007744|PDB:5WLW, ECO:0007744|PDB:6NZU, ECO:0007744|PDB:6UXE, ECO:0007744|PDB:6W1D, ECO:0007744|PDB:6WI2, ECO:0007744|PDB:6WIH, ECO:0007744|PDB:7RTK

Chain	Residue	Details
A	LYS258

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site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Cysteine persulfide => ECO:0000305|PubMed:18650437, ECO:0000305|PubMed:23593335

Chain	Residue	Details
A	CYS381

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