Structure of PDB 4lmh Chain B

Receptor sequence
>4lmhB (length=694) Species: 211586 (Shewanella oneidensis MR-1) [Search protein sequence]
VGVNINSTSTLKAKFTNATVDAGKVTVNFTLENANGVAVLGLTKDHDLRF
GIAQLTPVKEKVGETEADRGYQWQAYINAKKEPGTVPSGVDNLNPSTQFQ
ANVESANKCDTCLVDHGDGSYSYTYQVNVANVTEPVKVTYSADATQRATM
ELELPQLAANAHFDWQPSTGKTEGIQTRNVVSIQACYTCHQPESLALHGG
RRIDIENCASCHTATSGDPESGNSIEFTYMIHAIHKGGERHTFDATGAQV
PAPYKIIGYGGKVIDYGKVHYPQKPAADCAACHVEGAGAPANADLFKADL
SNQACIGCHTEKPSAHHSSTDCMACHNATKPYGGTGSAAKRHGDVMKAYN
DSLGYKAKFSNIGIKNNALTFDVQILDNKDQPIGKEFISDPSAYTKSSIY
FSWGIDKDYPAYTAGSRYSDRGFALSNSKVSTYNEATKTFTIDSTNSNLK
LPADLTGMNVELYAGVATCFNKGGYGVEDVVATPCSTDTRYAYIQDQPFR
FKWNGTDTNSAAEKRRAIIDTAKCSGCHNKEIVHYDNGVNCQACHTPDKG
LKTDNTYPGTKVPTSFAWKAHESEGHYLKYAGVQSGTVLKTDCATCHTAD
KSNVVTGIALGRSPERAWLYGDIKNNGAVIWVSSDAGACLSCHQKYLSDA
AKSHIETNGGILNGTSAADVQTRASESCATCHTPSQLMEAHGNK
3D structure
PDB4lmh Insights into electron transfer at the microbe-mineral interface: the X-ray crystal structures of Shewanella oneidensis MtrC and OmcA
ChainB
Resolution2.7 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 B C228 C231 H232 L237 H277 Y308 V311 Y313 P314 C324 L620 G624 V625 S627 T629 C186 C189 H190 L195 H235 Y266 V269 Y271 P272 C282 L578 G582 V583 S585 T587
BS02 HEC B Q142 L239 H240 R244 N249 C250 C253 H254 D260 I267 M272 I299 I306 Y308 Q100 L197 H198 R202 N207 C208 C211 H212 D218 I225 M230 I257 I264 Y266
BS03 HEC B R220 V222 F269 T270 I273 H274 H277 C324 H325 L337 F338 S343 H384 R178 V180 F227 T228 I231 H232 H235 C282 H283 L295 F296 S301 H342
BS04 HEC B H274 K278 A318 C347 C350 H351 H368 A380 R383 H384 V387 H232 K236 A276 C305 C308 H309 H326 A338 R341 H342 V345
BS05 HEC B H351 P355 H359 S361 T362 D363 C364 C367 H368 Y374 T377 R383 Y517 H309 P313 H317 S319 T320 D321 C322 C325 H326 Y332 T335 R341 Y475
BS06 HEC B H312 P314 K565 C566 C569 H570 I574 F608 S615 G617 H618 V630 T637 C638 H270 P272 K523 C524 C527 H528 I532 F566 S573 G575 H576 V588 T595 C596
BS07 HEC B Y442 Y460 V575 H576 Y577 C583 C586 H587 K591 T606 K611 Y400 Y418 V533 H534 Y535 C541 C544 H545 K549 T564 K569
BS08 HEC B R557 R558 I560 I561 F608 A612 H613 H618 K632 C635 C638 H639 I650 R658 H733 R515 R516 I518 I519 F566 A570 H571 H576 K590 C593 C596 H597 I608 R616 H691
BS09 HEC B H613 K632 L652 C681 C684 H685 H724 L729 H733 H571 K590 L610 C639 C642 H643 H682 L687 H691
BS10 HEC B A678 H696 I697 N700 C720 C723 H724 A636 H654 I655 N658 C678 C681 H682
BS11 CA B D260 E262 I299 D218 E220 I257
Gene Ontology
Molecular Function
GO:0046872 metal ion binding
Biological Process
GO:0071281 cellular response to iron ion

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4lmh, PDBe:4lmh, PDBj:4lmh
PDBsum4lmh
PubMed
UniProtQ8EG33

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