Structure of PDB 5obo Chain A

Receptor sequence

>5oboA (length=456) Species: 658080 (Ralstonia sp. 5_2_56FAA)

KLPGDFGPPRGEPIHAVLTSPPLVPPPVNRTYPAKVIVELEVVEKEMQIS
EGVSYTFWTFGGTVPGSFIRVRQGDTVEFHLKNHPSSKMPHNINLHGVTG
PGGGAASSFTAPGHESQFTFKALNEGIYVYHCATAPVGMHIANGMYGLIL
VEPPEGLPKVDHEYYVMQGDFYTAGKYREKGLQPFDMEKAIDERPSYVLF
NGAEGALTGDKALHAKVGETVRIFVGNGGPNLVSSFHVIGAIFDQVRYEG
GTNVQKNVQTTLIPAGGAAVVKFTARVPGSYVLVDHSIFRAFNKGAMAIL
KIDGAENKLVYSGKELDSVYLGDRAAPNMSAVTKATQASVSGTLTVQDQV
QAGRALFAGTCSVCHQGNGAGLPGVFPPLAKSDFLAADPKRAMNIVLHGL
NGKIKVNGQEYDSVMPPMTQLNDDEVANILTYVLNSWDNPGGRVSAEDVK
KVRAQP

3D structure

• PDB: 5obo Activation of redox tyrosine switch is required for ligand binding at the catalytic site in heme-cu nitrite reductases
• Chain: A
• Resolution: 1.89 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H94 N97 H99 H134 C135 H143 M148 H240 Q262 T263 H289
• Catalytic site (residue number reindexed from 1): H91 N94 H96 H131 C132 H140 M145 H237 Q259 T260 H286
• Enzyme Commision number: 1.7.2.1: nitrite reductase (NO-forming).

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	CU	A	H94 C135 H143 M148	H91 C132 H140 M145
BS02	CU	A	H99 H134	H96 H131
BS03	HEC	A	T363 C364 C367 H368 P380 P381 L382 S385 F387 I398 N404 G405 S416 M418 M421	T360 C361 C364 H365 P377 P378 L379 S382 F384 I395 N401 G402 S413 M415 M418
BS04	NO2	A	N97 H99 H134	N94 H96 H131

Gene Ontology

Molecular Function

• GO:0005507 copper ion binding
• GO:0009055 electron transfer activity
• GO:0016491 oxidoreductase activity
• GO:0020037 heme binding
• GO:0046872 metal ion binding
• GO:0050421 nitrite reductase (NO-forming) activity

Cellular Component

• GO:0042597 periplasmic space

External links

• PDB: RCSB:5obo, PDBe:5obo, PDBj:5obo
• PDBsum: 5obo
• UniProt: U3G913