Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7ER7

Crystal structure of hyman Biliverdin IX-beta reductase B with Tamibarotene (A80)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004074	molecular_function	biliverdin reductase [NAD(P)+] activity
A	0005515	molecular_function	protein binding
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0008752	molecular_function	FMN reductase (NAD(P)H) activity
A	0016491	molecular_function	oxidoreductase activity
A	0016740	molecular_function	transferase activity
A	0030219	biological_process	megakaryocyte differentiation
A	0035605	molecular_function	peptidyl-cysteine S-nitrosylase activity
A	0042167	biological_process	heme catabolic process
A	0042602	molecular_function	riboflavin reductase (NADPH) activity
A	0043231	cellular_component	intracellular membrane-bounded organelle
A	0046627	biological_process	negative regulation of insulin receptor signaling pathway
A	0052873	molecular_function	FMN reductase (NADPH) activity
A	0052874	molecular_function	FMN reductase (NADH) activity
A	0070062	cellular_component	extracellular exosome
A	0106276	molecular_function	biliberdin reductase (NAD+) activity
A	0106277	molecular_function	biliverdin reductase (NADP+) activity
B	0004074	molecular_function	biliverdin reductase [NAD(P)+] activity
B	0005515	molecular_function	protein binding
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0008752	molecular_function	FMN reductase (NAD(P)H) activity
B	0016491	molecular_function	oxidoreductase activity
B	0016740	molecular_function	transferase activity
B	0030219	biological_process	megakaryocyte differentiation
B	0035605	molecular_function	peptidyl-cysteine S-nitrosylase activity
B	0042167	biological_process	heme catabolic process
B	0042602	molecular_function	riboflavin reductase (NADPH) activity
B	0043231	cellular_component	intracellular membrane-bounded organelle
B	0046627	biological_process	negative regulation of insulin receptor signaling pathway
B	0052873	molecular_function	FMN reductase (NADPH) activity
B	0052874	molecular_function	FMN reductase (NADH) activity
B	0070062	cellular_component	extracellular exosome
B	0106276	molecular_function	biliberdin reductase (NAD+) activity
B	0106277	molecular_function	biliverdin reductase (NADP+) activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	36
Details	binding site for residue NAP A 401

Chain	Residue
A	GLY10
A	LEU74
A	LEU75
A	GLY76
A	ARG78
A	VAL86
A	MET87
A	CYS109
A	THR110
A	HIS132
A	PRO151
A	THR12
A	PRO152
A	HIS153
A	ILE154
A	A80402
A	HOH508
A	HOH515
A	HOH528
A	HOH548
A	HOH556
A	HOH560
A	GLY13
A	HOH565
A	HOH576
A	HOH594
A	HOH595
A	HOH600
B	SER82
B	HOH538
A	GLN14
A	THR15
A	ARG35
A	ARG39
A	ASP54
A	VAL55

site_id	AC2
Number of Residues	11
Details	binding site for residue A80 A 402

Chain	Residue
A	MET1
A	LEU81
A	PHE113
A	TRP116
A	PRO152
A	HIS153
A	ARG170
A	ARG174
A	TYR200
A	NAP401
A	HOH548

site_id	AC3
Number of Residues	5
Details	binding site for residue SO4 A 403

Chain	Residue
A	SER173
A	ARG174
A	HOH509
A	HOH525
A	HOH531

site_id	AC4
Number of Residues	26
Details	binding site for residue NAP B 401

Chain	Residue
A	ASP36
A	SER38
A	HOH501
B	GLY10
B	THR12
B	GLY13
B	GLN14
B	THR15
B	ARG35
B	ARG39
B	ASP54
B	VAL55
B	LEU75
B	GLY76
B	ARG78
B	CYS109
B	THR110
B	SER111
B	HIS132
B	PRO151
B	PRO152
B	ILE154
B	SO4406
B	HOH511
B	HOH563
B	HOH572

site_id	AC5
Number of Residues	9
Details	binding site for residue SO4 B 402

Chain	Residue
A	ARG140
A	HOH616
B	HIS153
B	GLY155
B	ASP156
B	GLN157
B	VAL175
B	HOH507
B	HOH546

site_id	AC6
Number of Residues	4
Details	binding site for residue SO4 B 403

Chain	Residue
A	ALA48
A	HIS49
B	LYS137
B	HOH501

site_id	AC7
Number of Residues	3
Details	binding site for residue SO4 B 404

Chain	Residue
A	HIS183
B	LYS4
B	HOH512

site_id	AC8
Number of Residues	3
Details	binding site for residue SO4 B 405

Chain	Residue
B	ALA26
B	TYR28
B	HOH509

site_id	AC9
Number of Residues	5
Details	binding site for residue SO4 B 406

Chain	Residue
B	HIS153
B	NAP401
B	HOH529
A	ARG134
B	ARG78

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: S-nitroso-cysteine intermediate; for S-nitroso-CoA-dependent nitrosyltransferase activity => ECO:0000269\|PubMed:38056462

Chain	Residue	Details
A	CYS109
A	CYS188
B	CYS109
B	CYS188

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:11224564, ECO:0000269\|PubMed:29487133, ECO:0000269\|PubMed:34957824, ECO:0007744\|PDB:1HDO, ECO:0007744\|PDB:5OOG, ECO:0007744\|PDB:5OOH, ECO:0007744\|PDB:7ER7

Chain	Residue	Details
A	GLY10
B	GLY10

site_id	SWS_FT_FI3
Number of Residues	16
Details	BINDING: BINDING => ECO:0000269\|PubMed:11224564, ECO:0000269\|PubMed:29487133, ECO:0000269\|PubMed:32246827, ECO:0000269\|PubMed:34957824, ECO:0007744\|PDB:1HDO, ECO:0007744\|PDB:1HE2, ECO:0007744\|PDB:1HE3, ECO:0007744\|PDB:1HE4, ECO:0007744\|PDB:1HE5, ECO:0007744\|PDB:5OOG, ECO:0007744\|PDB:5OOH, ECO:0007744\|PDB:6OPL, ECO:0007744\|PDB:7ER6, ECO:0007744\|PDB:7ER7, ECO:0007744\|PDB:7ER8, ECO:0007744\|PDB:7ER9, ECO:0007744\|PDB:7ERA, ECO:0007744\|PDB:7ERB, ECO:0007744\|PDB:7ERC, ECO:0007744\|PDB:7ERD, ECO:0007744\|PDB:7ERE

Chain	Residue	Details
A	THR12
B	THR15
B	ARG35
B	ASP54
B	VAL55
B	GLY76
B	ARG78
B	MET87
A	THR15
A	ARG35
A	ASP54
A	VAL55
A	GLY76
A	ARG78
A	MET87
B	THR12

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:11224564, ECO:0000269\|PubMed:32246827, ECO:0000269\|PubMed:34957824, ECO:0007744\|PDB:1HDO, ECO:0007744\|PDB:1HE2, ECO:0007744\|PDB:1HE3, ECO:0007744\|PDB:1HE4, ECO:0007744\|PDB:1HE5, ECO:0007744\|PDB:5OOG, ECO:0007744\|PDB:5OOH, ECO:0007744\|PDB:6OPL, ECO:0007744\|PDB:7ER6, ECO:0007744\|PDB:7ER7, ECO:0007744\|PDB:7ER8, ECO:0007744\|PDB:7ER9, ECO:0007744\|PDB:7ERA, ECO:0007744\|PDB:7ERB, ECO:0007744\|PDB:7ERC, ECO:0007744\|PDB:7ERD, ECO:0007744\|PDB:7ERE

Chain	Residue	Details
A	GLY13
B	GLY13

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:11224564, ECO:0000269\|PubMed:29487133, ECO:0000269\|PubMed:34957824, ECO:0007744\|PDB:1HDO, ECO:0007744\|PDB:1HE2, ECO:0007744\|PDB:1HE3, ECO:0007744\|PDB:1HE4, ECO:0007744\|PDB:1HE5, ECO:0007744\|PDB:5OOG, ECO:0007744\|PDB:5OOH, ECO:0007744\|PDB:7ER6, ECO:0007744\|PDB:7ER7, ECO:0007744\|PDB:7ER8, ECO:0007744\|PDB:7ER9, ECO:0007744\|PDB:7ERA, ECO:0007744\|PDB:7ERB, ECO:0007744\|PDB:7ERC, ECO:0007744\|PDB:7ERD, ECO:0007744\|PDB:7ERE

Chain	Residue	Details
A	GLN14
A	ILE154
B	GLN14
B	ILE154

site_id	SWS_FT_FI6
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:34957824, ECO:0007744\|PDB:7ER6, ECO:0007744\|PDB:7ER9, ECO:0007744\|PDB:7ERA, ECO:0007744\|PDB:7ERB, ECO:0007744\|PDB:7ERD, ECO:0007744\|PDB:7ERE

Chain	Residue	Details
A	SER38
B	SER38

site_id	SWS_FT_FI7
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:29487133, ECO:0000269\|PubMed:32246827, ECO:0000269\|PubMed:34957824, ECO:0007744\|PDB:5OOH, ECO:0007744\|PDB:6OPL, ECO:0007744\|PDB:7ER6, ECO:0007744\|PDB:7ER7, ECO:0007744\|PDB:7ER8, ECO:0007744\|PDB:7ER9, ECO:0007744\|PDB:7ERA, ECO:0007744\|PDB:7ERB, ECO:0007744\|PDB:7ERC, ECO:0007744\|PDB:7ERE

Chain	Residue	Details
A	ARG39
B	ARG39

site_id	SWS_FT_FI8
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:11224564, ECO:0000269\|PubMed:32246827, ECO:0000269\|PubMed:34957824, ECO:0007744\|PDB:1HDO, ECO:0007744\|PDB:1HE2, ECO:0007744\|PDB:1HE3, ECO:0007744\|PDB:1HE4, ECO:0007744\|PDB:1HE5, ECO:0007744\|PDB:6OPL, ECO:0007744\|PDB:7ER6, ECO:0007744\|PDB:7ER7, ECO:0007744\|PDB:7ER8, ECO:0007744\|PDB:7ER9, ECO:0007744\|PDB:7ERA, ECO:0007744\|PDB:7ERB, ECO:0007744\|PDB:7ERC, ECO:0007744\|PDB:7ERD, ECO:0007744\|PDB:7ERE

Chain	Residue	Details
A	LEU75
B	LEU75

site_id	SWS_FT_FI9
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:11224564, ECO:0000269\|PubMed:29487133, ECO:0000269\|PubMed:32246827, ECO:0000269\|PubMed:34957824, ECO:0007744\|PDB:1HDO, ECO:0007744\|PDB:1HE2, ECO:0007744\|PDB:1HE3, ECO:0007744\|PDB:1HE4, ECO:0007744\|PDB:1HE5, ECO:0007744\|PDB:5OOH, ECO:0007744\|PDB:6OPL, ECO:0007744\|PDB:7ER6, ECO:0007744\|PDB:7ER7, ECO:0007744\|PDB:7ER8, ECO:0007744\|PDB:7ER9, ECO:0007744\|PDB:7ERA, ECO:0007744\|PDB:7ERB, ECO:0007744\|PDB:7ERC, ECO:0007744\|PDB:7ERD, ECO:0007744\|PDB:7ERE

Chain	Residue	Details
A	CYS109
B	CYS109

site_id	SWS_FT_FI10
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:11224564, ECO:0000269\|PubMed:29487133, ECO:0000269\|PubMed:32246827, ECO:0000269\|PubMed:34957824, ECO:0007744\|PDB:1HE3, ECO:0007744\|PDB:5OOG, ECO:0007744\|PDB:5OOH, ECO:0007744\|PDB:6OPL, ECO:0007744\|PDB:7ER8, ECO:0007744\|PDB:7ER9, ECO:0007744\|PDB:7ERB, ECO:0007744\|PDB:7ERC

Chain	Residue	Details
A	HIS132
B	HIS132

site_id	SWS_FT_FI11
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:32246827, ECO:0000269\|PubMed:34957824, ECO:0007744\|PDB:6OPL, ECO:0007744\|PDB:7ERB, ECO:0007744\|PDB:7ERD

Chain	Residue	Details
A	HIS153
B	HIS153

site_id	SWS_FT_FI12
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:24275569

Chain	Residue	Details
A	SER42
B	SER42

site_id	SWS_FT_FI13
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	SER82
B	SER82

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)