5AC2

human aldehyde dehydrogenase 1A1 with duocarmycin analog

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0001523	biological_process	retinoid metabolic process
A	0001758	molecular_function	retinal dehydrogenase (NAD+) activity
A	0004029	molecular_function	aldehyde dehydrogenase (NAD+) activity
A	0005096	molecular_function	GTPase activator activity
A	0005497	molecular_function	androgen binding
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006081	biological_process	aldehyde metabolic process
A	0006629	biological_process	lipid metabolic process
A	0009449	biological_process	gamma-aminobutyric acid biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
A	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A	0018479	molecular_function	benzaldehyde dehydrogenase (NAD+) activity
A	0019145	molecular_function	aminobutyraldehyde dehydrogenase (NAD+) activity
A	0030392	biological_process	fructosamine catabolic process
A	0030424	cellular_component	axon
A	0036438	biological_process	maintenance of lens transparency
A	0042572	biological_process	retinol metabolic process
A	0045202	cellular_component	synapse
A	0051287	molecular_function	NAD binding
A	0070062	cellular_component	extracellular exosome
A	0106373	molecular_function	3-deoxyglucosone dehydrogenase activity
A	0110095	biological_process	cellular detoxification of aldehyde
A	0120163	biological_process	negative regulation of cold-induced thermogenesis
A	0140087	molecular_function	acetaldehyde dehydrogenase (NAD+) activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE K9P A 1502

Chain	Residue
A	PHE171
A	TYR457
A	GLY458
A	MET175
A	TRP178
A	PHE290
A	HIS293
A	GLY294
A	TYR297
A	CYS302
A	ILE304

---

site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE YB A 1503

Chain	Residue
A	ASP283

---

site_id	AC3
Number of Residues	29
Details	BINDING SITE FOR RESIDUE TXE A 1504

Chain	Residue
A	ILE166
A	ILE167
A	PRO168
A	TRP169
A	ASN170
A	LYS193
A	ALA195
A	GLU196
A	GLY226
A	GLY230
A	ALA231
A	PHE244
A	THR245
A	GLY246
A	SER247
A	VAL250
A	GLU269
A	GLY271
A	CYS303
A	GLU349
A	GLN350
A	LYS353
A	GLU400
A	PHE402
A	YB1508
A	HOH2085
A	HOH2089
A	HOH2122
A	HOH2123

---

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE YB A 1507

Chain	Residue
A	HOH2016
A	HOH2017
A	HOH2018
A	HOH2124
A	HOH2130
A	HOH2164
A	HOH2164
A	HOH2165

---

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE YB A 1508

Chain	Residue
A	TXE1504
A	HOH2089
A	HOH2091
A	HOH2122
A	HOH2123
A	HOH2163
A	HOH2166
A	HOH2167

---

Functional Information from PROSITE/UniProt

site_id	PS00070
Number of Residues	12
Details	ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FyHQGQCCIAAS

Chain	Residue	Details
A	PHE296-SER307

---

site_id	PS00687
Number of Residues	8
Details	ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKSP

Chain	Residue	Details
A	LEU268-PRO275

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	165
Details	Region: {"description":"Mediates interaction with PRMT3","evidences":[{"source":"PubMed","id":"33495566","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10007","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10008","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3676276","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10007","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10008","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3676276","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"25450233","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25634381","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4WB9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4X4L","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P20000","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	9
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---