Structure of PDB 5la3 Chain A

Receptor sequence

>5la3A (length=574) Species: 1501 (Clostridium pasteurianum) [Search protein sequence]

KTIIINGVQFNTDEDTTILKFARDNNIDISALCFLNNCNNDINKCEICTV
EVEGTGLVTACDTLIEDGMIINTNSDAVNEKIKSRISQLLDIHEFKCGPC
NRRENCEFLKLVIKYKARASKPFLPKDKTEYVDERSKSLTVDRTKCLLCG
RCVNACGKNTETYAMKFLNKNGKTIIGAEDEKCFDDTNCLLCGQCIIACP
VAALSEKSHMDRVKNALNAPEKHVIVAMAPSVRASIGELFNMGFGVDVTG
KIYTALRQLGFDKIFDINFGADMTIMEAATELVQRIENNGPFPMFTSCCP
GWVRQAENYYPELLNNLSSAKSPQQIFGTASKTYYPSISGLDPKNVFTVT
VMPCTSKKFEADRPQMEKDGLRDIDAVITTRELAKMIKDAKIPFAKLEDS
EADPAMGEYSGAGAIFGATGGVMEAALRSAKDFAENAELEDIEYKQVRGL
NGIKEAEVEINNNKYNVAVINGASNLFKFMKSGMINEKQYHFIEVMACHG
GCVNGGGQPHVNPKDLEKVDIKKVRASVLYNQDEHLSKRKSHENTALVKM
YQNYFGKPGEGRAHEILHFKYKKS

3D structure

PDB

5la3 Accumulating the hydride state in the catalytic cycle of [FeFe]-hydrogenases.

Chain

Resolution

2.29 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	A279 E282 C299 S319 K358 E361 Q366 C503
Catalytic site (residue number reindexed from 1)	A278 E281 C298 S318 K357 E360 Q365 C502
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	A229 P230 S231 C298 P323 Q324 M352 P353 K357 F416 M496 C502
BS02	SF4	A	C300 C355 A498 C499 C503	C299 C354 A497 C498 C502
BS03	SF4	A	C157 A165 M166 C190 L191 L192 C193 G194 Q195 C196	C156 A164 M165 C189 L190 L191 C192 G193 Q194 C195
BS04	SF4	A	C147 L148 L149 C150 G151 C153 I177 C200 P201 A204 L205	C146 L147 L148 C149 G150 C152 I176 C199 P200 A203 L204
BS05	SF4	A	H94 F96 K97 C98 C101 R104 C107 K146 V202	H93 F95 K96 C97 C100 R103 C106 K145 V201
BS06	FES	A	C34 F35 C46 E47 C49 C62	C33 F34 C45 E46 C48 C61

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:5la3, PDBe:5la3, PDBj:5la3
PDBsum	5la3
PubMed	28722011
UniProt	P29166\|PHF1_CLOPA Iron hydrogenase 1

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