Structure of PDB 2vpz Chain A

Receptor sequence

>2vpzA (length=734) Species: 262724 (Thermus thermophilus HB27) [Search protein sequence]

APWYAQEVKSVYQICEGCFWRCGIVAHAVGNRVYKVEGYEANPKSRGRLC
PRGQGAPQTTYDPDRLKRPLIRVEGSQRGEGKYRVATWEEALDHIAKKML
EIREKYGPEAIAFFGHGTGDYWFVDFLPAAWGSPNAAKPSVSLCTAPREV
ASQWVFGRPIGGHEPIDWENARYIVLIGHHIGEDTHNTQLQDFALALKNG
AKVVVVDPRFSTAAAKAHRWLPIKPGTDTALLLAWIHVLIYEDLYDKEYV
AKYTVGFEELKAHVKDFTPEWAEKHTEIPAQVIREVAREMAAHKPRAVLP
PTRHNVWYGDDTYRVMALLYVNVLLGNYGRPGGFYIAQSPYLEKYPLPPL
PLEPAAGGCSGPSGGDHEPEGFKPRADKGKFFARSTAIQELIEPMITGEP
YPIKGLFAYGINLFHSIPNVPRTKEALKNLDLYVAIDVLPQEHVMWADVI
LPEATYLERYDDFVLVAHKTPFIQLRTPAHEPLFDTKPGWWIARELGLRL
GLEQYFPWKTIEEYLETRLQSLGLDLETMKGMGTLVQRGKPWLEDWEKEG
RLPFGTASGKIELYCQRFKEAGHQPLPVFTPPEEPPEGFYRLLYGRSPVH
TFARTQNNWVLMEMDPENEVWIHKEEAKRLGLKEGDYVMLVNQDGVKEGP
VRVKPTARIRKDCVYIVHGFGHKAPLMRLAHGRGASDNYLQTRYKLDPIS
GGAGLRVNFVRLEKAERPRLPSLTGLAKRPFDER

3D structure

PDB

2vpz Molecular Mechanism of Energy Conservation in Polysulfide Respiration

Chain

Resolution

2.4 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	R81 H145 D149 K167 C173 T174 R332 Y364 P369 Y370 P380
Catalytic site (residue number reindexed from 1)	R52 H116 D120 K138 C144 T145 R303 Y335 P340 Y341 P351
Enzyme Commision number	1.-.-.-

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)
BS01	SF4	A	C44 G46 C47 W49 C51 C79 R81 G82 N216	C15 G17 C18 W20 C22 C50 R52 G53 N187
BS02	MGD	A	H145 L172 C173 G439 N441 H444 S445 I465 D466 Q470 E482 R488 Y623 R625 F631 A632 R633 H697 D716 N717	H116 L143 C144 G410 N412 H415 S416 I436 D437 Q441 E453 R459 Y594 R596 F602 A603 R604 H668 D687 N688
BS03	MGD	A	R81 G207 H209 D213 T214 H215 V235 D236 P237 R238 D257 T331 R332 H333 W336 Y337 R625 H629 T630 F631 R735	R52 G178 H180 D184 T185 H186 V206 D207 P208 R209 D228 T302 R303 H304 W307 Y308 R596 H600 T601 F602 R706

Gene Ontology

	Molecular Function
GO:0016491	oxidoreductase activity
GO:0043546	molybdopterin cofactor binding
GO:0046872	metal ion binding
GO:0051539	4 iron, 4 sulfur cluster binding

View graph for
Molecular Function

External links

PDB	RCSB:2vpz, PDBe:2vpz, PDBj:2vpz
PDBsum	2vpz
PubMed	18536726
UniProt	Q72LA4

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