Structure of PDB 6n6p Chain A

Receptor sequence

>6n6pA (length=573) Species: 1501 (Clostridium pasteurianum) [Search protein sequence]

MKTIIINGVQFNTDEDTTILKFARDNNIDISALCFLNNCNNDINKCEICT
VEVEGTGLVTACDTLIEDGMIINTNSDAVNEKIKSRISQLLDIHEFKCGP
CNRRENCEFLKLVIKYKARASKPFLPKDKTEYVDERSKSLTVDRTKCLLC
GRCVNACGKNTETYAMKFLNKNGKTIIGAEDEKCFDDTNCLLCGQCIIAC
PVAALSEKSHMDRVKNALNAPEKHVIVAMAPSVRASIGELFNMGFGVDVT
GKIYTALRQLGFDKIFDINFGADMTIMEEATELVQRIENNGPFPMFTSCC
PGWVRQAENYYPELLNNLSSAKSPQQIFGTASKTYYPSISGLDPKNVFTV
TVMPCTSKKFEADRPQMEKDGLRDIDAVITTRELAKMIKDAKIPFAKLED
SEADPAMGEYSGAGAIFGATGGVMEAALRSAKDFAENAELEDIEYKQVRG
LNGIKEAEVEINNNKYNVAVINGASNLFKFMKSGMINEKQYHFIEVMACH
GGCVNGGGQPHVNPKDLEKVDIKKVRASVLYNQDEHLSKRKSHENTALVK
MYQNYFGKPGEGRAHEILHFKYK

3D structure

PDB

6n6p Tuning Catalytic Bias of Hydrogen Gas Producing Hydrogenases.

Chain

Resolution

1.95 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	E279 E282 C299 S319 K358 E361 Q366 C503
Catalytic site (residue number reindexed from 1)	E279 E282 C299 S319 K358 E361 Q366 C503
Enzyme Commision number	1.12.7.2: ferredoxin hydrogenase.

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	402	A	A230 P231 S232 C299 P324 Q325 M353 P354 K358 F417 M497 C503 K573	A230 P231 S232 C299 P324 Q325 M353 P354 K358 F417 M497 C503 K573
BS02	SF4	A	C300 P301 C355 M497 C499 C503	C300 P301 C355 M497 C499 C503
BS03	SF4	A	C157 A165 M166 C190 L191 L192 C193 G194 C196	C157 A165 M166 C190 L191 L192 C193 G194 C196
BS04	SF4	A	C147 L148 L149 C150 G151 C153 I177 C200 P201 A204 L205	C147 L148 L149 C150 G151 C153 I177 C200 P201 A204 L205
BS05	SF4	A	H94 F96 K97 C98 C101 R104 C107 L110 V202	H94 F96 K97 C98 C101 R104 C107 L110 V202
BS06	FES	A	A32 C34 F35 K45 C46 E47 C49 C62	A32 C34 F35 K45 C46 E47 C49 C62

Gene Ontology

	Molecular Function
GO:0005506	iron ion binding
GO:0008901	ferredoxin hydrogenase activity
GO:0016491	oxidoreductase activity
GO:0046872	metal ion binding
GO:0051536	iron-sulfur cluster binding
GO:0051539	4 iron, 4 sulfur cluster binding

View graph for
Molecular Function

External links

PDB	RCSB:6n6p, PDBe:6n6p, PDBj:6n6p
PDBsum	6n6p
PubMed	31816235
UniProt	P29166\|PHF1_CLOPA Iron hydrogenase 1

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