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3PO0

Crystal structure of SAMP1 from Haloferax volcanii

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0031386molecular_functionprotein tag activity
A0032446biological_processprotein modification by small protein conjugation
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 88
ChainResidue
AALA41
AASP49
AHOH128
AHOH165

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CD A 89
ChainResidue
AHOH94
AASP55
AHIS56
AGLU64
AGLU70
AHOH93

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD A 90
ChainResidue
AGLU11
AASP30
AGLY87
AHOH171

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 91
ChainResidue
AGLU2
AASP49
AHOH160
AHOH176
AHOH177

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 92
ChainResidue
AGLU43
AGLU77
AHOH145
AHOH156
AHOH157
AHOH158

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Glycyl adenylate; alternate => ECO:0000269|PubMed:21368171
ChainResidueDetails
AGLY87

site_idSWS_FT_FI2
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins); alternate
ChainResidueDetails
AGLY87

221051

PDB entries from 2024-06-12

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