Structure of PDB 6ehq Chain M

Receptor sequence
>6ehqM (length=551) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
SQRITIDPVTRIEGHLRIDCEIENGVVSKAWASGTMWRGMEEIVKNRDPR
DAWMIVQRICGVCTTTHALSSVRAAESALNIDVPVNAQYIRNIILAAHTT
HDHIVHFYQLSALDWVDITSALQADPTKASEMLKGVSTWHLNSPEEFTKV
QNKIKDLVASGQLGIFANGYWGHPAMKLPPEVNLIAVAHYLQALECQRDA
NRVVALLGGKTPHIQNLAVGGVANPINLDGLGVLNLERLMYIKSFIDKLS
DFVEQVYKVDTAVIAAFYPEWLTRGKGAVNYLSVPEFPTDSKNGSFLFPG
GYIENADLSSYRPITSHSDEYLIKGIQESAKHSWYKDEAPQAPWEGTTIP
AYDGWSDDGKYSWVKSPTFYGKTVEVGPLANMLVKLAAGRESTQNKLNEI
VAIYQKLTGNTLEVAQLHSTLGRIIGRTVHCCELQDILQNQYSALITNIG
KGDHTTFVKPNIPATGEFKGVGFLEAPRGMLSHWMVIKDGIISNYQAVVP
STWNSGPRNFNDDVGPYEQSLVGTPVADPNKPLEVVRTIHSFDPCMACAV
H
3D structure
PDB6ehq The structure of hydrogenase-2 fromEscherichia coli: implications for H2-driven proton pumping.
ChainM
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E14 C61 C64 H68 R479 S502 C546 C549
Catalytic site (residue number reindexed from 1) E13 C60 C63 H67 R478 S501 C545 C548
Enzyme Commision number 1.12.99.6: hydrogenase (acceptor).
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 F3S M K211 Q216 K210 Q215
BS02 FCO M C64 H68 P478 R479 L482 V500 P501 S502 C549 C63 H67 P477 R478 L481 V499 P500 S501 C548
BS03 MG M E42 A498 H552 E41 A497 H551
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0008901 ferredoxin hydrogenase activity
GO:0016151 nickel cation binding
GO:0016491 oxidoreductase activity
GO:0033748 hydrogenase (acceptor) activity
GO:0046872 metal ion binding
Cellular Component
GO:0005886 plasma membrane

View graph for
Molecular Function

View graph for
Cellular Component
External links
PDB RCSB:6ehq, PDBe:6ehq, PDBj:6ehq
PDBsum6ehq
PubMed29555844
UniProtP0ACE0|MBHM_ECOLI Hydrogenase-2 large chain (Gene Name=hybC)

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