Structure of PDB 4apb Chain A

Receptor sequence
>4apbA (length=460) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
NYRIEHDTMGEVRVPAKALWRAQTQRAVENFPISGRGLERTQIRALGLLK
GACAQVNSDLGLLAPEKADAIIAAAAEIADGQHDDQFPIDVFQTGSGTSS
NMNTNEVIASIAAKGGVTLHPNDDVNMSQSSNDTFPTATHIAATEAAVAH
LIPALQQLHDALAAKALDWHTVVKSGRTHLMDAVPVTLGQEFSGYARQIE
AGIERVRACLPRLGELAIGGTAVGTGLNAPDDFGVRVVAVLVAQTGLSEL
RTAANSFEAQAARDGLVEASGALRTIAVSLTKIANDIRWMGSGPLTGLAE
IQLPDLQPGCSIMPGKVNPVLPEAVTQVAAQVIGNDAAIAWGGANGAFEL
NVYIPMMARNILESFKLLTNVSRLFAQRCIAGLTANVEHLRRLAESSPSI
VTPLNSAIGYEEAAAVAKQALKERKTIRQTVIDRGLIGDRLSIEDLDRRL
DVLAMAKAEQ
3D structure
PDB4apb Conformational Changes Upon Ligand Binding in the Essential Class II Fumarase Rv1098C from Mycobacterium Tuberculosis.
ChainA
Resolution1.94 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H187 C318 K324 E331
Catalytic site (residue number reindexed from 1) H179 C310 K316 E323
Enzyme Commision number 4.2.1.2: fumarate hydratase.
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 FUM A C318 S319 M321 K324 N326 C310 S311 M313 K316 N318
BS02 FUM A T106 S138 S139 N140 T98 S130 S131 N132
BS03 FUM A T186 H187 T178 H179
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004333 fumarate hydratase activity
GO:0016829 lyase activity
Biological Process
GO:0006099 tricarboxylic acid cycle
GO:0006106 fumarate metabolic process
Cellular Component
GO:0005576 extracellular region
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0009274 peptidoglycan-based cell wall

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:4apb, PDBe:4apb, PDBj:4apb
PDBsum4apb
PubMed22561013
UniProtP9WN93|FUMC_MYCTU Fumarate hydratase class II (Gene Name=fumC)

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