Structure of PDB 6qpx Chain A

Receptor sequence

>6qpxA (length=454) Species: 329 (Ralstonia pickettii)

LPGDFGPPRGEPIHAVLTSPPLVPPPVNRTYPAKVIVELEVVEKEMQISE
GVSYTFWTFGGTVPGSFIRVRQGDTVEFHLKNHPSSKMPHNIDLHGVTGP
GGGAASSFTAPGHESQFTFKALNEGIYVYHCATAPVGMHIANGMYGLILV
EPPEGLPKVDHEYYVMQGDFYTAGKYREKGLQPFDMEKAIDERPSYVLFN
GAEGALTGDKALHAKVGETVRIFVGNGGPNLVSSFHVIGAIFDQVRYEGG
TNVQKNVQTTLIPAGGAAVVKFTARVPGSYVLVDHSIFRAFNKGAMAILK
IDGAENKLVYSGKELDSVALGDRAAPNMSAVTKATQASVSGTLTVQDQVQ
AGRALFAGTCSVCHQGNGAGLPGVFPPLAKSDFLAADPKRAMNIVLHGLN
GKIKVNGQEYDSVMPPMTQLNDDEVANILTYVLNSWDNPGGRVSAEDVKK
VRAQ

3D structure

• PDB: 6qpx Unexpected Roles of a Tether Harboring a Tyrosine Gatekeeper Residue in Modular Nitrite Reductase Catalysis.
• Chain: A
• 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	A	H94 C135 H143 M148	H90 C131 H139 M144
BS02	CU	A	H99 H134	H95 H130
BS03	HEC	A	T363 C364 C367 H368 P380 P381 L382 S385 F387 N404 G405 I407 V409 Y414 S416 M418 M421	T359 C360 C363 H364 P376 P377 L378 S381 F383 N400 G401 I403 V405 Y410 S412 M414 M417
BS04	NO2	A	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