Structure of PDB 4lm8 Chain A

Receptor sequence

>4lm8A (length=626) Species: 211586 (Shewanella oneidensis MR-1) [Search protein sequence]

SIQTLNLDITKVSYENGAPMVTVFATNEADMPVIGLANLEIKKALQLIPE
GATGPGNSANWQGLGSSKSYVDNKNGSYTFKFDAFDSNKVFNAQLTQRFN
VVSAAGKLADGTTVPVAEMVEDFDGQGNAPQYTKNIVSHEVCASCHVEGE
KIYHQATEVETCISCHTQEFADGRGKPHVAFSHLIHNVHNANKAWGKDNK
IPTVAQNIVQDNCQVCHVESDMLTEAKNWSRIPTMEVCSSCHVDIDFAAG
KGHSQQLDNSNCIACHNSDWTAELHTAKTTATKNLINQYGIETTSTINTE
TKAATISVQVVDANGTAVDLKTILPKVQRLEIITNVGPNNATLGYSGKDS
IFAIKNGALDPKATINDAGKLVYTTTKDLKLGQNGADSDTAFSFVGWSMC
SSEGKFVDCADPAFDGVDVTKYTGMKADLAFATLSGKAPSTRHVDSVNMT
ACANCHTAEFEIHKGKQHAGFVMTEQLSHTQDANGKAIVGLDACVTCHTP
DGTYSFANRGALELKLHKKHVEDAYGLIGGNCASCHSDFNLESFKKKGAL
NTAAAADKTGLYSTPITATCTTCHTVGSQYMVHTKETLESFGAVVDGTKD
DATSAAQSETCFYCHTPTVADHTKVK

3D structure

PDB

4lm8 Redox Linked Flavin Sites in Extracellular Decaheme Proteins Involved in Microbe-Mineral Electron Transfer.

Chain

Resolution

1.8 Å

3D
structure

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Enzymatic activity

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)	Binding affinity
BS01	HEC	A	C186 C189 H190 I196 I229 V232 H233 K244 A249 I252 L571	C142 C145 H146 I152 I185 V188 H189 K200 A205 I208 L527
BS02	HEC	A	K86 I196 Y197 H198 Q199 A200 C206 C209 H210 F214 R218 K220 L228	K42 I152 Y153 H154 Q155 A156 C162 C165 H166 F170 R174 K176 L184
BS03	HEC	A	S102 I180 I229 H230 H233 D255 C257 C260 H261 N272 W273 V281 H319	S58 I136 I185 H186 H189 D211 C213 C216 H217 N228 W229 V237 H275
BS04	HEC	A	D255 C282 C285 H286 L318 H319 K322	D211 C238 C241 H242 L274 H275 K278
BS05	HEC	A	T278 M279 H286 F291 H297 Q300 N305 C306 C309 H310	T234 M235 H242 F247 H253 Q256 N261 C262 C265 H266
BS06	HEC	A	N251 I252 C496 C499 H500 F504 L535 L560 K563 H564 A568 I572	N207 I208 C452 C455 H456 F460 L491 L516 K519 H520 A524 I528
BS07	HEC	A	I377 F438 H507 C538 C541 H542 T547 Y548 N552 K559 K563	I333 F394 H463 C494 C497 H498 T503 Y504 N508 K515 K519
BS08	HEC	A	R486 H487 S490 L560 H561 H564 C576 C579 H580 F583 N584 H666	R442 H443 S446 L516 H517 H520 C532 C535 H536 F539 N540 H622
BS09	HEC	A	H561 C614 C617 H618 H659 H666 T667	H517 C570 C573 H574 H615 H622 T623
BS10	HEC	A	T611 H618 Y624 M625 V626 H627 F635 C655 C658 H659	T567 H574 Y580 M581 V582 H583 F591 C611 C614 H615
BS11	CA	A	D52 I53 E165	D8 I9 E121
BS12	CA	A	N231 N234 K237	N187 N190 K193
BS13	CA	A	D472 Q520	D428 Q476
BS14	CA	A	E162 E202	E118 E158

Gene Ontology

	Molecular Function
GO:0016491	oxidoreductase activity
GO:0046872	metal ion binding

View graph for
Molecular Function

External links

PDB	RCSB:4lm8, PDBe:4lm8, PDBj:4lm8
PDBsum	4lm8
PubMed	26126857
UniProt	Q8EG34

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