Structure of PDB 2h63 Chain D

Receptor sequence

>2h63D (length=285) Species: 9606 (Homo sapiens)

MRKFGVVVVGVGRAGSVRMRDLRNPHPSSAFLNLIGFVSRRELGSIDGVQ
QISLEDALSSQEVEVAYICSESSSHEDYIRQFLNAGKHVLVEYPMTLSLA
AAQELWELAEQKGKVLHEEHVELLMEEFAFLKKEVVGKDLLKGSLLFTAG
PLEEERFGFPAFSGISRLTWLVSLFGELSLVSATLEERYMKMTVCLETEK
KSPLSWIEEKGPGLKRNRYLSFHFKSGSLENVPNVGVNKNIFLKDQNIFV
QKLLGQFSEKELAAEKKRILHCLGLAEEIQKYCCS

3D structure

• PDB: 2h63 Crystal Structure of Human Biliverdin Reductase A
• Chain: D
• Resolution: 2.7 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): E97 Y98 E124 E127 S171 R172
• Catalytic site (residue number reindexed from 1): E92 Y93 E119 E122 S166 R167
• Enzyme Commision number: 1.3.1.24: biliverdin reductase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	NAP	D	G15 V16 G17 R18 A19 S44 R45 R46 C74 S75 H80 E97 Y98 E124 F162	G10 V11 G12 R13 A14 S39 R40 R41 C69 S70 H75 E92 Y93 E119 F157

Gene Ontology

Molecular Function

• GO:0000166 nucleotide binding
• GO:0003824 catalytic activity
• GO:0004074 biliverdin reductase [NAD(P)+] activity
• GO:0005515 protein binding
• GO:0008270 zinc ion binding
• GO:0016491 oxidoreductase activity
• GO:0046872 metal ion binding
• GO:0106276 biliberdin reductase (NAD+) activity
• GO:0106277 biliverdin reductase (NADP+) activity

Biological Process

• GO:0042167 heme catabolic process

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol
• GO:0070062 extracellular exosome

External links

• PDB: RCSB:2h63, PDBe:2h63, PDBj:2h63
• PDBsum: 2h63
• UniProt: P53004|BIEA_HUMAN Biliverdin reductase A (Gene Name=BLVRA)