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1MEJ

Human Glycinamide Ribonucleotide Transformylase domain at pH 8.5

Functional Information from GO Data
ChainGOidnamespacecontents
A0004644molecular_functionphosphoribosylglycinamide formyltransferase activity
A0006189biological_process'de novo' IMP biosynthetic process
A0009058biological_processbiosynthetic process
B0004644molecular_functionphosphoribosylglycinamide formyltransferase activity
B0006189biological_process'de novo' IMP biosynthetic process
B0009058biological_processbiosynthetic process
C0004644molecular_functionphosphoribosylglycinamide formyltransferase activity
C0006189biological_process'de novo' IMP biosynthetic process
C0009058biological_processbiosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PO4 B 450
ChainResidue
BGLY11
BHOH522
BSER12
BASN13
BLYS170
BHOH451
BHOH456
BHOH460
BHOH505
BHOH520

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 451
ChainResidue
ATHR10
AGLY11
ASER12
AASN13
ALYS170
AHOH474
AHOH492

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL C 452
ChainResidue
CTHR10
CGLY11
CSER12
CASN13
CHOH462

Functional Information from PROSITE/UniProt
site_idPS00373
Number of Residues24
DetailsGART Phosphoribosylglycinamide formyltransferase active site. GcTVhFVaEdVDaGqiIlqeavpV
ChainResidueDetails
BGLY133-VAL156

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P08179
ChainResidueDetails
BHIS108
AHIS108
CHIS108

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:12450384, ECO:0000269|PubMed:16026156, ECO:0007744|PDB:1MEN, ECO:0007744|PDB:1ZLY
ChainResidueDetails
BGLY11
BLYS170
AGLY11
ALYS170
CGLY11
CLYS170

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:12755606, ECO:0007744|PDB:1NJS
ChainResidueDetails
BARG64
BASN106
AARG64
AASN106
CARG64
CASN106

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:12755606, ECO:0000305|PubMed:16026156, ECO:0007744|PDB:1NJS, ECO:0007744|PDB:1ZLY
ChainResidueDetails
BMET89
BALA140
AMET89
AALA140
CMET89
CALA140

site_idSWS_FT_FI5
Number of Residues3
DetailsSITE: Raises pKa of active site His => ECO:0000250|UniProtKB:P08179
ChainResidueDetails
BASP144
AASP144
CASP144

218853

PDB entries from 2024-04-24

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