Structure of PDB 6laa Chain A

Receptor sequence

>6laaA (length=753) Species: 876478 (Tepidiphilus thermophilus) [Search protein sequence]

PVHRLAEDFDPFQDAYMADPAQFVRWAREQVPIFYAPKLNYWVVTRYDTI
KQIFRDPVTFSPSNVLQSFAQPSAEVRQVLERYGYAFNRTLVNEDEPMHL
ERRRVLMEPFASEHLAEHEPMVRELVRRAVNRFIDTGRADLVDQMIWEVP
FTVALHFLGVDDDDREKMRRFAIAHTVNAFGRPSPEEQLAVAETVGQFWQ
FCGEVLEKMRRTADGPGWMRYSIRQQKLYPDVVTDSYLHSMMQAIIVAAH
ETTVFATTNALKTLLEHETVWREICADPSLIPAAAEECLRYNGPVAGWRR
RTTREVEVEGVRLPVGANILMVVASANHDSAHFDDPEFFDIGRSNASEHL
NFGYGAHQCLGRNLGRMEMQIMIEELSRRLPHMRLAEQRFDYLHNVSFRA
PRHLWVEWDPAQNPERRDPDILRLRQPVRIGPPRAKDVVRTMEVAAVERP
SEDIVVLHLTRPDRRPLPRWSPGAHIDIECGEPDRSRQYSLCSDPENRDA
WRVAVQRDPASRGGSRWIHEEVRPGMLLRVRGPRNSFRLDEHAPRYLFLA
GGIGITPIMTMAARAKELGTDYELHYSVRSRTSLIFVDELRQIHGDRLHV
YVSEEGVRNDLAALIRRASAGTQIYACGPQRMLDTLERLIENRPEVTLRV
EHFFGEPSHLDPAKERPFQVVLRNSGLTVEVPADKTLLEVLRAYNIEVQS
DCEEGLCGTCEVSVVEGEVDHRDSVLTRAERRENRRMMCCCSRAKTERLV
LDL

3D structure

PDB

6laa Structural insight into the electron transfer pathway of a self-sufficient P450 monooxygenase.

Chain

Resolution

2.13 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	V203 E277 T278 C385 L386 G387
Catalytic site (residue number reindexed from 1)	V177 E251 T252 C359 L360 G361
Enzyme Commision number	?

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	HEM	A	F80 L117 V118 H125 R129 A275 T278 T279 W324 N377 F378 G379 H383 C385 G387	F54 L91 V92 H99 R103 A249 T252 T253 W298 N351 F352 G353 H357 C359 G361
BS02	FES	A	S726 C728 E729 G731 C733 G734 C736 C766	S700 C702 E703 G705 C707 G708 C710 C740
BS03	FMN	A	R513 Q514 Y515 S516 Q532 S537 R538 G540 S541 I579 E677 F679	R487 Q488 Y489 S490 Q506 S511 R512 G514 S515 I553 E651 F653
BS04	CO3	A	T116 L117 V118 M267	T90 L91 V92 M241

Gene Ontology

	Molecular Function
GO:0000166	nucleotide binding
GO:0004497	monooxygenase activity
GO:0005506	iron ion binding
GO:0016491	oxidoreductase activity
GO:0016705	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0020037	heme binding
GO:0046872	metal ion binding
GO:0051536	iron-sulfur cluster binding
GO:0051537	2 iron, 2 sulfur cluster binding

View graph for
Molecular Function

External links

PDB	RCSB:6laa, PDBe:6laa, PDBj:6laa
PDBsum	6laa
PubMed	32472090
UniProt	A0A0K6ITW2

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