Structure of PDB 2zoo Chain A

Receptor sequence

>2zooA (length=438) Species: 326442 (Pseudoalteromonas translucida TAC125)

LKTEQAILTPPPMVPPAINRDHSAKVVINLETREQVGRIADGVEYVFWSF
GETVPGSFIRVREGDEIEFNLSNHPSSKMPHNIDLHAVTGPGGGAESSFT
APGHTSTFNFKALNPGLYIYHCATAPVGMHIANGMYGLILVEPKEGLAPV
DREYYLVQGDFYTKGEFGEAGLQPFDMAKAIDEDADYVVFNGSVGSTTDE
NSLTAKVGETVRLYIGNGGPNLVSSFHVIGEIFDTVYVEGGSLKNHNVQT
TLIPAGGAAIVEFKVEVPGTFILVDHSIFRAFNKGALAMLKVEGPDDHSI
FTGKTAENVYLPEGSAIQSLDNTFTKITANNKDEQIRFGQRVYEANCMAC
HQANGEGIPGAFPPLAKSDYLNNNPLLGVNAIIKGLSGPIKVNNVNYNGV
MPAMNLNDEDIANVITFVLNNWDNAGGKVSAEQVAKQR

3D structure

• PDB: 2zoo Electron transfer processes within and between proteins containing the HEME C and blue Cu
• Chain: A
• Resolution: 1.95 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H84 D87 H89 H124 C125 H133 M138 H230 Q252 T253 H279
• Catalytic site (residue number reindexed from 1): H81 D84 H86 H121 C122 H130 M135 H227 Q249 T250 H276
• 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	H84 C125 H133 M138	H81 C122 H130 M135
BS02	CU	A	H89 H124	H86 H121
BS03	HEM	A	C350 C353 H354 F365 P366 P367 L368 S371 Y373 I385 L389 S390 G391 I393 V395 Y400 N401 G402 V403 M404	C347 C350 H351 F362 P363 P364 L365 S368 Y370 I382 L386 S387 G388 I390 V392 Y397 N398 G399 V400 M401

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

Biological Process

• GO:0019333 denitrification pathway
• GO:0042128 nitrate assimilation

Cellular Component

• GO:0042597 periplasmic space

External links

• PDB: RCSB:2zoo, PDBe:2zoo, PDBj:2zoo
• PDBsum: 2zoo
• UniProt: Q3IGF7