Structure of PDB 6hbe Chain B

Receptor sequence
>6hbeB (length=425) Species: 743525 (Thermus scotoductus SA-01) [Search protein sequence]
AERHFTLEARSSIFEVDQGVYLRGFSFNDMSPGPMLVVEEGDTVHITLRN
LDNVTHGLSIHAANTQTSRFLGNVQPGETREFSFTADFPGVFMYHCAPGG
HGIMAHTMGGQFGMIVVEPKEKYRMERELGRGPDLKLYIIQSEAYASGRD
FYDGKALYVMFNGRNFRYVDEPIPVRPGDYLRIYFLNVGPNLTSTLHVVG
GIFEYMYYQGNPKNLVVGAQTALAGPSDSWVIEWRVPPVEGDYTLVTHVF
GTAIKGALGILRAKKDAPRIPEVRAEGVPGVKEIPASAKRVVDPYGLASP
GHEHTVRVPLDPALAQPVAVGAKALEPLPVTVQMVGNSFYPKVLEIPVGT
TVEFVNEDVFDLLEGERTGRHDAVVIDVQGPEPFVTPKLGHGERYRITFT
KPGEYVYICSIHPYMKGIIRVYEPL
3D structure
PDB6hbe A three-domain copper-nitrite reductase with a unique sensing loop.
ChainB
Resolution1.63 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H75 S78 H80 H114 C115 H125 Q130 H216 Q239 T240 H267
Catalytic site (residue number reindexed from 1) H56 S59 H61 H95 C96 H106 Q111 H197 Q220 T221 H248
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 B H390 C428 H431 H371 C409 H412
BS02 CU B H80 H114 H61 H95
BS03 CU B H75 C115 H125 Q130 H56 C96 H106 Q111
BS04 CA B D36 Q37 D17 Q18
Gene Ontology
Molecular Function
GO:0005507 copper ion binding
GO:0009055 electron transfer activity
GO:0046872 metal ion binding
GO:0050421 nitrite reductase (NO-forming) activity

View graph for
Molecular Function
External links
PDB RCSB:6hbe, PDBe:6hbe, PDBj:6hbe
PDBsum6hbe
PubMed30867922
UniProtE8PLV7

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