1LC3

Crystal Structure of a Biliverdin Reductase Enzyme-Cofactor Complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000165	biological_process	MAPK cascade
A	0000166	molecular_function	nucleotide binding
A	0000978	molecular_function	RNA polymerase II cis-regulatory region sequence-specific DNA binding
A	0004074	molecular_function	biliverdin reductase [NAD(P)H] activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005977	biological_process	glycogen metabolic process
A	0006309	biological_process	apoptotic DNA fragmentation
A	0006629	biological_process	lipid metabolic process
A	0006631	biological_process	fatty acid metabolic process
A	0006641	biological_process	triglyceride metabolic process
A	0006935	biological_process	chemotaxis
A	0006954	biological_process	inflammatory response
A	0006955	biological_process	immune response
A	0006979	biological_process	response to oxidative stress
A	0007249	biological_process	canonical NF-kappaB signal transduction
A	0008270	molecular_function	zinc ion binding
A	0008286	biological_process	insulin receptor signaling pathway
A	0009986	cellular_component	cell surface
A	0010467	biological_process	gene expression
A	0016491	molecular_function	oxidoreductase activity
A	0032094	biological_process	response to food
A	0032496	biological_process	response to lipopolysaccharide
A	0034440	biological_process	lipid oxidation
A	0038178	biological_process	complement component C5a signaling pathway
A	0042167	biological_process	heme catabolic process
A	0042440	biological_process	pigment metabolic process
A	0042593	biological_process	glucose homeostasis
A	0043066	biological_process	negative regulation of apoptotic process
A	0043491	biological_process	phosphatidylinositol 3-kinase/protein kinase B signal transduction
A	0043583	biological_process	ear development
A	0046872	molecular_function	metal ion binding
A	0106276	molecular_function	biliberdin reductase (NADH) activity
A	0106277	molecular_function	biliverdin reductase (NADPH) activity
A	0160025	biological_process	sensory perception of itch
A	1901142	biological_process	insulin metabolic process
A	1903409	biological_process	reactive oxygen species biosynthetic process
A	1905237	biological_process	response to cyclosporin A

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 A 601

Chain	Residue
A	GLY15
A	VAL16
A	SER43
A	ARG44
A	ARG45
A	LYS209
A	HOH1095

---

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 A 602

Chain	Residue
A	ALA104
A	SER285
A	LYS289
A	NAD901
A	HOH1023
A	HOH1075
A	SER102
A	PHE103

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 A 604

Chain	Residue
A	PHE151
A	ARG171
A	ARG224
A	NAD900

---

site_id	AC4
Number of Residues	18
Details	BINDING SITE FOR RESIDUE NAD A 900

Chain	Residue
A	ARG18
A	ALA19
A	SER74
A	SER76
A	HIS79
A	GLU96
A	TYR97
A	PRO98
A	GLU123
A	LEU156
A	PHE161
A	SER167
A	PO4604
A	HOH1005
A	HOH1025
A	HOH1107
A	HOH1150
A	HOH1218

---

site_id	AC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE NAD A 901

Chain	Residue
A	MET2
A	ILE3
A	GLU66
A	PHE103
A	GLN107
A	LYS223
A	VAL245
A	GLN264
A	LYS289
A	GLN293
A	PO4602
A	HOH1052
A	HOH1091
A	HOH1178

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12079357","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LC3","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P53004","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P53004","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P53004","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P53004","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	6
Details	Annotated By Reference To The Literature 1gcu

Chain	Residue	Details
A	TYR97
A	GLU126
A	SER170
A	GLU123
A	GLU96
A	ARG171

---

site_id	MCSA1
Number of Residues	6
Details	M-CSA 566

Chain	Residue	Details
A	GLU96	electrostatic stabiliser
A	TYR97	electrostatic stabiliser, proton acceptor, proton donor
A	GLU123	electrostatic stabiliser
A	GLU126	electrostatic stabiliser
A	SER170	electrostatic stabiliser
A	ARG171	electrostatic stabiliser

---