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4J1O

Crystal structure of an enolase (mandelate racemase subgroup) from paracococus denitrificans pd1222 (target nysgrc-012907) with bound l-proline betaine (substrate)

Functional Information from GO Data
ChainGOidnamespacecontents
A0006579biological_processamino-acid betaine catabolic process
A0016853molecular_functionisomerase activity
A0016855molecular_functionracemase and epimerase activity, acting on amino acids and derivatives
A0046872molecular_functionmetal ion binding
A0047661molecular_functionamino-acid racemase activity
B0006579biological_processamino-acid betaine catabolic process
B0016853molecular_functionisomerase activity
B0016855molecular_functionracemase and epimerase activity, acting on amino acids and derivatives
B0046872molecular_functionmetal ion binding
B0047661molecular_functionamino-acid racemase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 401
ChainResidue
AASP194
AGLU219
AASP242
APBE412
AHOH503

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 402
ChainResidue
AHOH603
AHOH638
AHOH537
AHOH549
AHOH595
AHOH600

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 403
ChainResidue
ASER369
AHOH551
AHOH784
AHOH851
BGLN142

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 404
ChainResidue
AARG315

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 406
ChainResidue
AALA44

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE IOD A 407
ChainResidue
AHOH570
AHOH590
AHOH698

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 408
ChainResidue
ATRP46

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IOD A 409
ChainResidue
AGLN31
AALA61

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 411
ChainResidue
AASN335
AGLY336
AILE337
AARG338
AASP345
ALEU346
APRO347
AHOH546
AHOH633

site_idBC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PBE A 412
ChainResidue
ATYR56
ATYR135
AALA137
AGLN162
ALYS164
AASP194
AASN196
AGLU219
AASP242
ALYS266
AMG401
AHOH676

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 401
ChainResidue
BASP194
BGLU219
BASP242
BPBE407
BHOH509

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 402
ChainResidue
BHOH588
BHOH645
BHOH709
BHOH744
BHOH772
BHOH782

site_idBC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD B 403
ChainResidue
BARG315

site_idBC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD B 404
ChainResidue
BALA61

site_idBC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IOD B 406
ChainResidue
BHOH615
BHOH643

site_idBC7
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PBE B 407
ChainResidue
BTYR56
BTYR135
BGLN162
BLYS164
BASP194
BASN196
BGLU219
BASP242
BLYS266
BALA295
BMG401
BHOH680

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250
ChainResidueDetails
ALYS164
ALYS266
BLYS164
BLYS266

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING:
ChainResidueDetails
ATYR56
BGLU219
BASP242
BALA295
AGLN162
AASP194
AGLU219
AASP242
AALA295
BTYR56
BGLN162
BASP194

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PDB entries from 2025-06-18

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