1LC3

Crystal Structure of a Biliverdin Reductase Enzyme-Cofactor Complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003824	molecular_function	catalytic activity
A	0004074	molecular_function	biliverdin reductase (NAD(P)H) activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0008270	molecular_function	zinc ion binding
A	0016491	molecular_function	oxidoreductase activity
A	0042167	biological_process	heme catabolic process
A	0046872	molecular_function	metal ion binding
A	0106276	molecular_function	biliberdin reductase NAD+ activity
A	0106277	molecular_function	biliverdin reductase (NADPH) activity

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	4
Details	BINDING: BINDING => ECO:0000269|PubMed:12079357, ECO:0007744|PDB:1LC3

Chain	Residue	Details
A	ARG18
A	SER76
A	TYR97
A	SER167

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P53004

Chain	Residue	Details
A	HIS279
A	CYS280
A	CYS291
A	HIS292

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903

Chain	Residue	Details
A	SER154

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P53004

Chain	Residue	Details
A	THR173

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P53004

Chain	Residue	Details
A	SER177

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P53004

Chain	Residue	Details
A	LYS247
A	LYS252

---

Catalytic Information from CSA

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

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