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4A35

Crystal structure of human Mitochondrial enolase superfamily member 1 (ENOSF1)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005575cellular_componentcellular_component
A0005739cellular_componentmitochondrion
A0009063biological_processamino acid catabolic process
A0016052biological_processcarbohydrate catabolic process
A0016829molecular_functionlyase activity
A0016836molecular_functionhydro-lyase activity
A0016853molecular_functionisomerase activity
A0046872molecular_functionmetal ion binding
A0050023molecular_functionL-fuconate dehydratase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 1445
ChainResidue
AASP254
AGLU280
AGLU309
AHOH2387
AHOH2389
AHOH2418

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 1446
ChainResidue
ASER381
ASER383
AARG387
ATYR191
AASP376
ATYR377

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 1447
ChainResidue
AARG19
ATYR432
ATRP438
ALEU442
AHOH2076
AHOH2117
AHOH2590
AHOH2591

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1448
ChainResidue
ATHR22
ASER23
AGLY26
AHIS27
AGLU181
AHOH2326

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 1449
ChainResidue
ASER23
AASP37
AGLN185
AHOH2330
AHOH2590

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1450
ChainResidue
APRO21
ATYR377
ASER383
ALEU384
AHOH2514
AHOH2592

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 1451
ChainResidue
AARG222
ALEU277
AASN386
AARG387
AVAL388
AGLU436
ALYS440
AHOH2384
AHOH2517

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 1452
ChainResidue
AGLY94
AARG97
AHOH2176
AHOH2593

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 1453
ChainResidue
AASP161
AASP167
ALYS351
AHOH2296
AHOH2594

Functional Information from PROSITE/UniProt
site_idPS00909
Number of Residues32
DetailsMR_MLE_2 Mandelate racemase / muconate lactonizing enzyme family signature 2. LmmDaNqrwdvpeAvewmskLakfkplwIEEP
ChainResidueDetails
ALEU251-PRO282

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:Q8P3K2
ChainResidueDetails
ALYS226

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255
ChainResidueDetails
AHIS359

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q8P3K2
ChainResidueDetails
AGLY28
ATYR38
ALYS224
AASN256
AGLU280
AGLU309
AHIS359
AGLU390

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:24697329
ChainResidueDetails
AASP254

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:15994970
ChainResidueDetails
ASER152

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PDB entries from 2024-08-07

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