Structure of PDB 6qpx Chain I

Receptor sequence

>6qpxI (length=455) Species: 329 (Ralstonia pickettii)

LPGDFGPPRGEPIHAVLTSPPLVPPPVNRTYPAKVIVELEVVEKEMQISE
GVSYTFWTFGGTVPGSFIRVRQGDTVEFHLKNHPSSKMPHNIDLHGVTGP
GGGAASSFTAPGHESQFTFKALNEGIYVYHCATAPVGMHIANGMYGLILV
EPPEGLPKVDHEYYVMQGDFYTAGKYREKGLQPFDMEKAIDERPSYVLFN
GAEGALTGDKALHAKVGETVRIFVGNGGPNLVSSFHVIGAIFDQVRYEGG
TNVQKNVQTTLIPAGGAAVVKFTARVPGSYVLVDHSIFRAFNKGAMAILK
IDGAENKLVYSGKELDSVALGDRAAPNMSAVTKATQASVSGTLTVQDQVQ
AGRALFAGTCSVCHQGNGAGLPGVFPPLAKSDFLAADPKRAMNIVLHGLN
GKIKVNGQEYDSVMPPMTQLNDDEVANILTYVLNSWDNPGGRVSAEDVKK
VRAQP

3D structure

• PDB: 6qpx Unexpected Roles of a Tether Harboring a Tyrosine Gatekeeper Residue in Modular Nitrite Reductase Catalysis.
• Chain: I
• Resolution: 1.7 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H94 D97 H99 H134 C135 H143 M148 H240 Q262 T263 H289
• Catalytic site (residue number reindexed from 1): H90 D93 H95 H130 C131 H139 M144 H236 Q258 T259 H285
• 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	I	H94 C135 H143 M148	H90 C131 H139 M144
BS02	CU	I	H99 H134	H95 H130
BS03	HEC	I	T363 C364 C367 H368 P380 P381 L382 S385 F387 N404 G405 S416 M418 M421	T359 C360 C363 H364 P376 P377 L378 S381 F383 N400 G401 S412 M414 M417
BS04	NO2	I	D97 H99 H134	D93 H95 H130

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:6qpx, PDBe:6qpx, PDBj:6qpx
• PDBsum: 6qpx
• PubMed: 32051772
• UniProt: I6NAW4