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4MVA

1.43 Angstrom Resolution Crystal Structure of Triosephosphate Isomerase (tpiA) from Escherichia coli in Complex with Acetyl Phosphate.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004807molecular_functiontriose-phosphate isomerase activity
A0006096biological_processglycolytic process
B0004807molecular_functiontriose-phosphate isomerase activity
B0006096biological_processglycolytic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL A 301
ChainResidue
AGLU21
ALEU22
AASN25
AALA239
AHOH535
AHOH595

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE UVW A 302
ChainResidue
AGLY234
AHOH427
AHOH429
AHOH438
AHOH441
AHOH651
AHOH702
AHOH835
AHOH836
ALYS11
ASER212
AGLY233

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 A 303
ChainResidue
AARG16
AHOH839
BARG52

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 304
ChainResidue
AHIS17
AARG52
AHOH740
AHOH837

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE UVW B 301
ChainResidue
BLYS11
BILE172
BSER212
BGLY233
BGLY234
BPEG303
BHOH435
BHOH559
BHOH570
BHOH756

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 302
ChainResidue
ASER177
AALA178
ATHR179
BASN214
BSER216
BASN217

site_idAC7
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PEG B 303
ChainResidue
BLYS11
BHIS95
BGLY233
BGLY234
BUVW301
BHOH403
BHOH435
BHOH519
BHOH570
BHOH684
BHOH756

Functional Information from PROSITE/UniProt
site_idPS00171
Number of Residues11
DetailsTIM_1 Triosephosphate isomerase active site. AYEPVWAIGTG
ChainResidueDetails
AALA165-GLY175

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PDB entries from 2024-09-11

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